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500ug
| 产品编号 | bs-12463P |
| 英文名称 | phospho-CRYAB (Ser59) Antibody Blocking Peptide |
| 中文名称 | 磷酸化热休克蛋白β5/αb晶体蛋白质/α-晶体蛋白b链封闭多肽 |
| 英文别名 | alpha B Crystallin (phospho S59); alpha B Crystallin (phospho Ser59); p-alpha B Crystallin (S59); p-alpha B Crystallin (Ser59); AACRYA; Alpha B crystallin; Alpha crystallin B chain; Alpha crystallin B chain; Alpha(B) crystallin; Alpha(B)-crystallin; Alpha-crystallin B chain; CRYA2; CRYAB; CRYAB_HUMAN; Crystallin alpha B; Crystallin alpha polypeptide 2; CTPP 2; CTPP2; Heat shock 20 kD like protein; Heat shock protein beta 5; Heat shock protein beta-5; HSPB5; NY REN 27 antigen; Renal carcinoma antigen NY REN 27; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component. |
| 纯化方法 | HPLC |
| 研究领域 | Cancer > Cancer Metabolism > Cellular metabolic process Metabolism > Types of disease > Cancer Neuroscience > Neurotransmission > Receptors / Channels > Tyrosine Kinase Receptors Neuroscience > Sensory System > Visual system Signal Transduction > Protein Phosphorylation > Tyrosine Kinases |
| 亚基 | Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin. |
| 亚细胞定位 | Cytoplasm. Nucleus. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. |
| 组织特异性 | Lens as well as other tissues. |
| 相似性 | Belongs to the small heat shock protein (HSP20) family. |
| 功能 | May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. |
| 保存条件 | Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008]. |
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phospho-CRYAB (Ser59) Antibody Blocking Peptide(bs-12463P)-500ug
￥1080
