PYK2 Rabbit Recombinant mAb Datasheet

生物描述

特异性	PYK2 Rabbit Recombinant mAb detects endogenous level of total PYK2.
背景	Proline-rich tyrosine kinase 2 (PYK2) is a cytoplasmic, non-receptor tyrosine kinase implicated in multiple signaling pathways. PYK2 and FAK comprise the focal adhesion kinase subfamily of non-receptor tyrosine kinases. PYK2 and FAK are large multidomain proteins containing an N-terminal FERM domain, a central catalytic domain, and a C-terminal segment containing dual proline rich (PR) subdomains and a focal adhesion targeting (FAT) region. While FAK is widely expressed, PYK2 expression is relatively restricted with highest levels in brain and the hematopoeitic system. Unlike FAK, optimal PYK2 activation is dependent on Ca2+ mobilization. The catalytic activity of Pyk2 is regulated by phosphorylation. Pyk2 has four major sites of tyrosine phosphorylation, Tyr-402, Tyr-579, Tyr-580, and Tyr-881. Tyrosine 402 is an autophosphorylation site that, once phosphorylated, can bind to the SH2 domain of Src family kinases (SFK). The current model for the activation of this kinase is that upon stimulation, Pyk2 becomes autophosphorylated as a result of trans-autophosphorylation, which allows for the recruitment of SFK. SFK phosphorylate additional tyrosine residues within the protein thus enhancing catalytic activity (Tyr-579/Tyr-580) and providing a new docking site (Tyr-881) for SH2 domain-containing proteins. The focal adhesion kinases FAK and Pyk2 are uniquely situated to act as critical mediators for the activation of signaling pathways that regulate cell migration, proliferation, and survival.

特异性

PYK2 Rabbit Recombinant mAb detects endogenous level of total PYK2.

背景

Proline-rich tyrosine kinase 2 (PYK2) is a cytoplasmic, non-receptor tyrosine kinase implicated in multiple signaling pathways. PYK2 and FAK comprise the focal adhesion kinase subfamily of non-receptor tyrosine kinases. PYK2 and FAK are large multidomain proteins containing an N-terminal FERM domain, a central catalytic domain, and a C-terminal segment containing dual proline rich (PR) subdomains and a focal adhesion targeting (FAT) region. While FAK is widely expressed, PYK2 expression is relatively restricted with highest levels in brain and the hematopoeitic system. Unlike FAK, optimal PYK2 activation is dependent on Ca2+ mobilization. The catalytic activity of Pyk2 is regulated by phosphorylation. Pyk2 has four major sites of tyrosine phosphorylation, Tyr-402, Tyr-579, Tyr-580, and Tyr-881. Tyrosine 402 is an autophosphorylation site that, once phosphorylated, can bind to the SH2 domain of Src family kinases (SFK). The current model for the activation of this kinase is that upon stimulation, Pyk2 becomes autophosphorylated as a result of trans-autophosphorylation, which allows for the recruitment of SFK. SFK phosphorylate additional tyrosine residues within the protein thus enhancing catalytic activity (Tyr-579/Tyr-580) and providing a new docking site (Tyr-881) for SH2 domain-containing proteins. The focal adhesion kinases FAK and Pyk2 are uniquely situated to act as critical mediators for the activation of signaling pathways that regulate cell migration, proliferation, and survival.

使用信息

抗体应用

WB ,ELISA,ELISA

稀释比例

WB

1:1000

反应性

Human Mouse Rat

MW (kDa)

116kDa

抗体类型

Rabbit

储存液配方

10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide.

储存条件
(自收到货起)

Store at –20°C.

文献参考

Application Data

WB

Validated by Selleck