蛋白名称
Tyrosine-protein kinase SYK
免疫原
Synthesized phospho-peptide around the phosphorylation site of human Syk (phospho Tyr352)
特异性
Phospho-Syk (Y352) Polyclonal Antibody detects endogenous levels of Syk protein only when phosphorylated at Y352.
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
来源
Polyclonal, Rabbit,IgG
稀释比例
Western Blot: 1/500 - 1/2000. ELISA: 1/10000. Not yet tested in other applications.
纯化工艺
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
其他名称
SYK; Tyrosine-protein kinase SYK; Spleen tyrosine kinase; p72-Syk
背景
This gene encodes a member of the family of non-receptor type Tyr protein kinases. This protein is widely expressed in hematopoietic cells and is involved in coupling activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation, and phagocytosis. It is thought to be a modulator of epithelial cell growth and a potential tumour suppressor in human breast carcinomas. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010],
功能
catalytic activity:ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.,function:Positive effector of BCR-stimulated responses. Couples the B-cell antigen receptor (BCR) to the mobilization of calcium ion either through a phosphoinositide 3-kinase-dependent pathway, when not phosphorylated on tyrosines of the linker region, or through a phospholipase C-gamma-dependent pathway, when phosphorylated on Tyr-348 and Tyr-352. Thus the differential phosphorylation of Syk can determine the pathway by which BCR is coupled to the regulation of intracellular calcium ion.,PTM:Autophosphorylated.,PTM:Phosphorylation on Tyr-323 creates a binding site for c-Cbl, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling.,PTM:Phosphorylation on Tyr-348 and Tyr-352 enhances the phosphorylation and activation of phospholipase C-gamma and the early phas
