Datasheet

生物描述

特异性	Phospho-Raf1 (S259) Rabbit Recombinant mAb detects endogenous levels of phosphorylated Raf1 (S259).
背景	The Raf-1 kinase is an important signaling molecule, functioning in the Ras pathway to transmit mitogenic, differentiative, and oncogenic signals to the downstream kinases MEK and ERK. The regulation of Raf-1 activity is complex, involving inter- and intramolecular protein interactions as well as direct phosphorylation. In a quiescent cell, Raf-1 exists in an inactive state in the cytosol. The inactive conformation of Raf-1 is maintained by autoinhibitory interactions occurring between the N-terminal regulatory and the C-terminal catalytic domains and by the binding of a 14-3-3 dimer that contacts two phosphorylation sites, S259 and S621. That is, Raf-1 in quiescent cells was highly phosphorylated on two sites, S259 and S621. Binding of 14-3-3 proteins to Raf-1 molecules phosphorylates on S259 and S621 is thought to maintain Raf-1 in an inactive, autoinhibited conformation. Typically, the activation of Raf-1 is initiated by its interaction with Ras, which leads to the relocalization of cytosolic Raf-1 to the plasma membrane. Ras binding also promotes conformational changes that relieve Raf-1 autoinhibition and facilitate the phoshorylation of activating sites. These activating sites are found in the Raf-1 catalytic domain and include S338, Y341, T491, and S494.

特异性

Phospho-Raf1 (S259) Rabbit Recombinant mAb detects endogenous levels of phosphorylated Raf1 (S259).

背景

The Raf-1 kinase is an important signaling molecule, functioning in the Ras pathway to transmit mitogenic, differentiative, and oncogenic signals to the downstream kinases MEK and ERK. The regulation of Raf-1 activity is complex, involving inter- and intramolecular protein interactions as well as direct phosphorylation. In a quiescent cell, Raf-1 exists in an inactive state in the cytosol. The inactive conformation of Raf-1 is maintained by autoinhibitory interactions occurring between the N-terminal regulatory and the C-terminal catalytic domains and by the binding of a 14-3-3 dimer that contacts two phosphorylation sites, S259 and S621. That is, Raf-1 in quiescent cells was highly phosphorylated on two sites, S259 and S621. Binding of 14-3-3 proteins to Raf-1 molecules phosphorylates on S259 and S621 is thought to maintain Raf-1 in an inactive, autoinhibited conformation. Typically, the activation of Raf-1 is initiated by its interaction with Ras, which leads to the relocalization of cytosolic Raf-1 to the plasma membrane. Ras binding also promotes conformational changes that relieve Raf-1 autoinhibition and facilitate the phoshorylation of activating sites. These activating sites are found in the Raf-1 catalytic domain and include S338, Y341, T491, and S494.

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)

73kDa

抗体类型

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