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ASPH Human/ 重组人天冬氨酸Beta-羟化酶
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ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
Synonyms AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. Introduction ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. Description ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. Source Escherichia Coli. Physical Appearance Sterile Filtered colorless solution. Formulation The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. Stability ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. Purity Greater than 90.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
ASPH Human/ 重组人天冬氨酸Beta-羟化酶
产品编号：ENZ-488
产品规格：5μg/20μg/1mg
产品规格：5μg/20μg/1mg
| Synonyms | AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH. |
| Introduction | ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters ａnd goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms （a ａnd f） include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, ａnd X, ａnd the complement factors C1R ａnd C1S. Further isoforms diverge mainly in the C-terminal sequence ａnd lack the hydroxylase domain, ａnd some have been localized to the endoplasmic ａnd sarcoplasmic reticulum. |
| Description | ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids （75-270 a.a.） ａnd having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag ａnd purified by conventional chromatography. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile Filtered colorless solution. |
| Formulation | The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT ａnd 10% glycerol. |
| Stability | ASPH although stable 4°C for 4 weeks, should be stored desiccated below -18°C. For long term storage it is recommended to add a carrier protein （0.1% HSA or BSA）. Please prevent freeze-thaw cycles. |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT. |
| Purity | Greater than 90.0% as determined by SDS-PAGE. |
| Usage | ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals. |
