The specific immunogen used to produce this antibody is proprietary information.

Antibody detects endogenous levels of syk protein only when phosphorylated at Tyr525/526 of human Syk or Tyr519/520 of mouse Syk. It also detects Syk protein when singly phosphorylated at Tyr526 of human Syk or Tyr520 of mouse Syk. The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites): ENyyKA

SYK

Tyrosine-protein kinase SYK

SYK ;
Tyrosine-protein kinase SYK ;
Spleen tyrosine kinase ;
p72-Syk

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],

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 phase of calcium ion mobilization via a phosphoinositide 3-kinase-independent pathway.,PTM:Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation.,similarity:Belongs to the protein kinase superfamily. Tyr protein kinase family.,similarity:Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.,similarity:Contains 1 protein kinase domain.,similarity:Contains 2 SH2 domains.,subunit:Interacts with CBL and SLA when it is phosphorylated. The interaction with SLA may link it to CBL, leading to its destruction. Interacts with phosphorylated NFAM1 (By similarity). Interacts with Epstein-Barr virus LMP2A. Interacts through its SH2 domains with the phosphorylated ITAM domain of CD79A which stimulates SYK autophosphorylation and activation. Interacts with FCRL3.,

Cell membrane . Cytoplasm, cytosol .

>>NF-kappa B signaling pathway ;
>>Phospholipase D signaling pathway ;
>>PI3K-Akt signaling pathway ;
>>Osteoclast differentiation ;
>>Platelet activation ;
>>Neutrophil extracellular trap formation ;
>>C-type lectin receptor signaling pathway ;
>>Natural killer cell mediated cytotoxicity ;
>>B cell receptor signaling pathway ;
>>Fc epsilon RI signaling pathway ;
>>Fc gamma R-mediated phagocytosis ;
>>Tuberculosis ;
>>Kaposi sarcoma-associated herpesvirus infection ;
>>Herpes simplex virus 1 infection ;
>>Epstein-Barr virus infection ;
>>Coronavirus disease - COVID-19 ;
>>Viral carcinogenesis