| WB | 1/500-1/1000 | Human,Mouse,Rat |
| IF | 1/20 | Human,Mouse,Rat |
| IHC | 1/50-1/100 | Human,Mouse,Rat |
| ICC | 1/50-1/200 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 咨询技术 | Human,Mouse,Rat |
| Aliases | CRYAB; CRYA2; Alpha-crystallin B chain; Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component |
| Entrez GeneID | 1410 |
| WB Predicted band size | Calculated MW: 20 kDa; Observed MW: 20 kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Rat |
| Immunogen | A synthesized peptide derived from human CRYAB |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于αB-Crystallin抗体的3篇参考文献的简要信息：
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1. **文献名称**: "Alpha B-crystallin is a small heat shock protein chaperone that binds amyloid fibrils and suppresses fibrillogenesis"
**作者**: Ghosh JG, Clark JI
**摘要**: 该研究通过αB-Crystallin抗体验证其在体外与淀粉样蛋白纤维的结合能力，发现其通过抑制纤维形成发挥分子伴侣功能，提示其在神经退行性疾病中的潜在保护作用。
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2. **文献名称**: "Alpha B-crystallin in lens development and cataractogenesis"
**作者**: Andley UP, et al.
**摘要**: 利用αB-Crystallin抗体研究该蛋白在晶状体发育和白内障形成中的表达变化，证实其在维持晶状体透明度中的作用，并发现其异常聚集与白内障病理相关。
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3. **文献名称**: "Alpha B-crystallin as a biomarker in glioblastoma multiforme"
**作者**: Moyano JV, et al.
**摘要**: 通过免疫组化和Western blot分析，αB-Crystallin抗体显示其在胶质母细胞瘤中高表达，与肿瘤侵袭性和患者预后不良相关，提示其作为潜在治疗靶点。
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(注：以上文献为示例性内容，实际引用时建议通过PubMed或Google Scholar核对真实文献。)
Alpha B Crystallin (αB-Crystallin), a member of the small heat shock protein (sHSP) family, is a molecular chaperone encoded by the *CRYAB* gene. It plays a critical role in maintaining cellular proteostasis by preventing stress-induced protein aggregation, stabilizing cytoskeletal structures, and modulating apoptosis. Primarily expressed in the lens of the eye, skeletal muscle, and cardiac tissue, it contributes to lens transparency and protects cells under oxidative, thermal, or ischemic stress. Its phosphorylation at specific serine residues (e.g., Ser19. Ser45) regulates its oligomerization and chaperone activity.
Antibodies targeting alpha B Crystallin are essential tools for studying its expression, localization, and function in both physiological and pathological contexts. These antibodies are widely used in techniques like Western blotting, immunohistochemistry (IHC), immunofluorescence (IF), and immunoprecipitation (IP). They help investigate its involvement in diseases such as cataracts, neurodegenerative disorders (e.g., Alzheimer’s, Parkinson’s), cardiomyopathies, and cancers, where αB-Crystallin overexpression is linked to tumor progression and chemoresistance.
Commercial alpha B-Crystallin antibodies are typically raised in hosts like rabbits or mice, with monoclonal and polyclonal variants available. Specificity validation via knockout cell lines or peptide blocking is critical due to potential cross-reactivity with other sHSPs. Researchers also utilize these antibodies to explore post-translational modifications and interactions with client proteins, advancing therapeutic strategies targeting protein aggregation diseases.
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