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Spleen tyrosine Kinase (SYK) (C-Term,pTyr526,pTyr527) antibody
|Synonyms||FLJ25043, FLJ37489, DKFZp313N1010, Syk, p72syk|
Human, Mouse (Murine)
Alternatives Immunohistochemistry (IHC)
|6 references available|
|Price||452.38 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 5 to 7 Business Days|
|Immunogen||Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human SYK (Tyrosine-protein kinase SYK)|
|Description||SYK (Tyrosine-protein kinase SYK) is a positive effector of BCR-stimulated responses. SYK 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. SYK interacts with CBL and SLA when it is phosphorylated. The interaction with SLA may link it to CBL, leading to its destruction. SYK interacts with phosphorylated NFAM1. SYK interacts with Epstein-Barr virus LMP2A. SYK interacts through its SH2 domains with the phosphorylated ITAM domain of CD79A which stimulates SYK autophosphorylation and activation. SYK interacts with FCRL3. 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. 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. Ubiquitinated by CBLB after BCR activation, which promotes proteasomal degradation. SYK belongs to the protein kinase superfamily, Tyr protein kinase family and SYK/ZAP-70 subfamily.|
|Restrictions||For Research Use only|
Yagi, Suzuki, Hasegawa et al.: "Cloning of the cDNA for the deleted syk kinase homologous to ZAP-70 from human basophilic leukemia cell line (KU812)." in: Biochemical and biophysical research communications, Vol. 200, Issue 1, pp. 28-34, 1994 (PubMed).
Law, Sidorenko, Chandran et al.: "Molecular cloning of human Syk. A B cell protein-tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex." in: The Journal of biological chemistry, Vol. 269, Issue 16, pp. 12310-9, 1994 (PubMed).
Deckert, Elly, Altman et al.: "Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases." in: The Journal of biological chemistry, Vol. 273, Issue 15, pp. 8867-74, 1998 (PubMed).
Tang, Sawasdikosol, Chang et al.: "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 17, pp. 9775-80, 1999 (PubMed).
Xu, Zhao, Zhao: "Molecular cloning and characterization of SPAP1, an inhibitory receptor." in: Biochemical and biophysical research communications, Vol. 280, Issue 3, pp. 768-75, 2001 (PubMed).
Rikova, Guo, Zeng et al.: "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." in: Cell, Vol. 131, Issue 6, pp. 1190-203, 2007 (PubMed).