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厦门慧嘉生物专业销售Prospec PRO-320 LLO/重组李斯特氏菌素O ASSAY ImmunoWay Santa Abcam Cst jackson Pierce Sigma Amresco Qiagen Cayman abnova millipore invitrogen merk ebioscience prospec peprotech细胞因子特价。等生物试剂产品。实验为大，诚信经营，为客户提供“质量的产品”和“质的服务"QQ: 1193953234 1048735792 或登陆（向客服人员索取原版说明书） http://www.biohj.com 欢迎广大老师来询！
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
LLO/重组李斯特氏菌素O
产品编号：PRO-320
产品规格：10μg/50μg/1mg
Synonyms Listeriolysin-O, LLO, hlyA. Introduction Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. Description Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Formulation The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. Stability LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C.
Please prevent freeze-thaw cycles. Purity Greater than 90.0% as determined by（a） Analysis by RP-HPLC.
（b） Analysis by SDS-PAGE. Activity LLO has a hemolytic activity 1.25x106 HU/mg.
2mM DTT is used to reactivate the toxin. Applications a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）.
b. Production of specific monoclonal antibodies （5）.
c. Detection of anti-listeriolysin O antibodies （6）. 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.
产品规格：10μg/50μg/1mg
| Synonyms | Listeriolysin-O, LLO, hlyA. |
| Introduction | Listeriolysin O （aka LLO） is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene ａnd composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents ａnd inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes （average pH ~ 5.9） of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, ａnd the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system ａnd antibodies. LLO also brings about dephosphorylation of histone H3 ａnd deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO ａnd is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST＇s supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO. |
| Description | Molecular weight of Listeriolysin O is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequence （accession number: AAF64524）. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile Filtered clear solution. |
| Formulation | The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, 1mM DTT, 5% glycerol ａnd 0.5M NaCl. |
| Stability | LLO although stable at room temperature for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. |
| Purity | Greater than 90.0% as determined by（a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. |
| Activity | LLO has a hemolytic activity 1.25x106 HU/mg. 2mM DTT is used to reactivate the toxin. |
| Applications | a. Cytosolic delivery of molecules, peptides, oligonucleodides ａnd plasmid DNA （4）. b. Production of specific monoclonal antibodies （5）. c. Detection of anti-listeriolysin O antibodies （6）. |
| 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. |
