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Myosin Light Chain (Ser-19), phospho-specific Antibody
Myosin Light Chain (Ser-19), phospho-specific Antibody
- 中文名称：
- Myosin Light Chain (Ser-19), phospho-specific Antibody
- 英文名称：
- Myosin Light Chain (Ser-19), phospho-specific 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：
- AAA71664
- 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：
- Rabbit
- 反应种属：
- Human, Rat, Mouse, Chicken
- 应用：
- ICC (Immunocytochemistry), 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:Polyclonal
同型:N/A
克隆号:N/A
特异性:This antibody was cross-adsorbed to MLC (a.a. 11-22) then affinity purified using phospho-MLC (Ser-19) peptide (without carrier). The antibody detects a 20kDa* band corresponding to the molecular weight of myosin light chain in human A431 treated with EGF and in mouse C2C12 treated with Calyculin A. This reactivity is not observed after lambda phosphatase treatment of MLC.
纯度:N/A
形式：Rabbit polyclonal, affinity-purified antibody is supplied in 100ul phosphate-buffered saline, 50% glycerol, 1mg/ml BSA, and 0.05% sodium azide.
浓度：N/A
- 说明书：
Both smooth muscle and nonmuscle myosin II activity is regulated by the phosphorylation state of the myosin regulatory light chain (MLC, MRLC, MLC20, Myl9). Phosphorylation of MLC at Thr-18 and Ser-19 activates myosin II motor activity and increases myosin filament stability. This activation has important roles in various cell motile processes. By contrast, other phosphorylation sites on MLC may inhibit myosin II activity. PKC phosphorylates Ser-1/Ser-2 and Thr-9 in MLC, and this phosphorylation decreases activated myosin II interaction with actin, as well as inhibits MLC interaction with the activation site kinase, myosin light-chain kinase. The Ser-1/Ser-2 region may be the major inhibitory site since Ser-1 is phosphorylated during PDGF-induced stress fiber disassembly and expression of unphosphorylatable MLC20 at the Ser-1/Ser-2 site suppresses this disassembly. Thus, inhibition of myosin II activity through phosphorylation of Ser-1/Ser-2 may have important roles in growth factor-induced reorganization of actomyosin filaments.
