本公司经销phospho-CDKN1A/P21 （Thr57），磷酸化p21蛋白抗体，克隆类型为polyclonal，宿主来源是Rabbit，phospho-CDKN1A/P21 （Thr57）磷酸化p21蛋白抗体可应用于WB、elisa、IP、IF、IHC等实验，欢迎垂询订购！

货号：BY-5238R
英文名称：Anti-phospho-CDKN1A/P21 （Thr57）
中文名称：磷酸化p21蛋白抗体
其他名称：Activating Fragment 1; CAP20; Cation chloride cotransporter-interacting protein 1; CDK Interacting Protein 1; CDK-interacting protein 1; CDKI; CDKN 1; CDKN1; CDKN1A; CIP1; Cyclin Dependent Kinase Inhibitor 1A; Cyclin-dependent kinase inhibitor 1; Cyclin-dependent kinase inhibitor 1A （P21）; Cyclin-dependent kinase inhibitor 1A （p21, Cip1）; DNA Synthesis Inhibitor; MDA 6; MDA-6; MDA6; Melanoma Differentiation Associated Protein 6; Melanoma differentiation-associated protein 6; Melanoma differentiation-associated protein; p21; P21 protein; p21CIP1; p21WAF; PIC1; SDI1; SLC12A9; WAF1; Wildtype p53 Activating Fragment 1; Wildtype p53-activated fragment 1.
抗体来源：Rabbit
克隆类型：polyclonal
蛋白分子量：predicted molecular weight: 18kDa
纯化方法：affinity purified by Protein A
交叉反应：hu, mo, rat
产品介绍：This gene encodes a potent cyclin-dependent kinase inhibitor. The encoded protein binds to ａnd inhibits the activity of cyclin-CDK2 or -CDK4 complexes, ａnd thus functions as a regulator of cell cycle progression at G1. The expression of this gene is tightly controlled by the tumor suppressor protein p53, through which this protein mediates the p53-dependent cell cycle G1 phase arrest in response to a variety of stress stimuli. This protein can interact with proliferating cell nuclear antigen （PCNA）, a DNA polymerase accessory factor, ａnd plays a regulatory role in S phase DNA replication ａnd DNA damage repair. This protein was reported to be specifically cleaved by CASP3-like caspases, which thus leads to a dramatic activation of CDK2, ａnd may be instrumental in the execution of apoptosis following caspase activation. Two alternatively spliced variants, which encode an identical protein, have been reported.Function : May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to ａnd inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates ａnd blocking cell cycle progression. Functions in the nuclear localization ａnd assembly of cyclin D-CDK4 complex ａnd promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex.Subunit : Interacts with HDAC1; the interaction is prevented by competitive binding of C10orf90/FATS to HDAC1 facilitating acetylation ａnd protein stabilization of CDKN1A/p21. Interacts with MKRN1. Interacts with PSMA3. Interacts with PCNA. Component of the ternary complex, cyclin D-CDK4-CDKN1A. Interacts （via its N-terminal domain） with CDK4; the interaction promotes the assembly of the cyclin D-CDK4 complex, its nuclear translocation ａnd promotes the cyclin D-dependent enzyme activity of CDK4. Binding to CDK2 leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Interacts with PIM1.Subcellular Location : Cytoplasmic ａnd Nuclear.Tissue Specificity : Expressed in spleen, liver ａnd lung. Not detected in kidney, colon, stomach or brain.Post-translational modifications : Phosphorylation of Thr-145 by Akt or of Ser-146 by PKC impairs binding to PCNA. Phosphorylation at Ser-114 by GSK3-beta enhances ubiquitination by the DCX（DTL） complex. Phosphorylation of Thr-145 by PIM2 enhances CDKN1A stability ａnd inhibits cell proliferation. Phosphorylation of Thr-145 by PIM1 results in the relocation of CDKN1A to the cytoplasm ａnd enhanced CDKN1A protein stability.Ubiquitinated by MKRN1; leading to polyubiquitination ａnd 26S proteasome-dependent degradation. Ubiquitinated by the DCX（DTL） complex, also named CRL4（CDT2） complex, leading to its degradation during S phase or following UV irradiation. Ubiquitination by the DCX（DTL） complex is essential to control replication licensing ａnd is PCNA-dependent: interacts with PCNA via its PIP-box, while the presence of the containing the ＇K+4＇ motif in the PIP box, recruit the DCX（DTL） complex, leading to its degradation.Acetylation leads to protein stability. Acetylated in vitro on Lys-141, Lys-154, Lys-161 ａnd Lys-163. Deacetylation by HDAC1 is prevented by competitive binding of C10orf90/FATS to HDAC1.Similarity : Belongs to the CDI family.Database links : UniProtKB/Swiss-Prot: P38936.3p21蛋白的过度表达与肿瘤的类型、恶性度、分期以及病人的预后密切相关。主要用于胃肠道癌肿、乳腺癌、肺癌等恶性肿瘤的研究。