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Talin (Rod domain) Antibody
Talin (Rod domain) Antibody
- 中文名称：
- Talin (Rod domain) Antibody
- 英文名称：
- Talin (Rod domain) Antibody
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA71718
- 规格：
- 0.1 mL|2x0.1 mL|3x0.1 mL|4x0.1 mL|5x0.1 mL
- 保存建议：
- Store at -20 degree C. Stable for 1 year.
- 货期：
- 6-8周
- 来源宿主：
- Mouse
- 反应种属：
- Human, Rat, Mouse, Chicken, Fish
- 应用：
- ICC (Immunocytochemistry), IP (Immunoprecipitation), ELISA, WB (Western Blot)
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 其他：
克隆性:Monoclonal
同型:IgG1
克隆号:[8D4]
特异性:The antibody detects a 240kDa* protein corresponding to the molecular mass of Talin on SDS-PAGE immunoblots of human A431, rat PC12, and rabbit fibroblast cells.
纯度:Protein A chromatography
形式：Mouse monoclonal antibody purified with protein A chromatography is supplied in 100ul phosphate-buffered saline, 50% glycerol, 1mg/ml BSA, and 0.05% sodium azide.
浓度：N/A
- 说明书：
Talin is an important cytoskeletal component of integrin adhesion sites. Calpins cleave talin precursor (240kDa) into an amino-terminal globular head domain of 47kDa and a carboxyl-terminal 190kDa rod domain. The talin head domain contains a FERM domain that binds integrins, PIP kinase (Type I), and FAK. The rod domain has several vinculin-binding sites, a second integrin-binding site, and two actin-binding sites. These talin protein-protein interactions are critical for integrin activation, focal adhesion formation, and cell migration. Talin regulation may occur through phosphorylation and regulated degradation. The talin head domain binds Smurf1, an E3 ubiquitin ligase, and this interaction leads to talin head ubiquitylation and degradation. Cdk5 can phosphorylate Ser-425 in the head domain, and this inhibits both binding to Smurf1 and subsequent degradation. The S425A talin mutant resists Cdk5 phosphorylation, increases susceptibility to Smurf1-mediated ubiquitylation, and inhibits cell migration. Thus, talin head phosphorylation may be important for regulating adhesion stability and cell migration.
