Product Pathways - Lymphocyte Signaling
Phospho-Syk (Tyr525/526) Antibody #2711
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W | H (M) (R) | 72 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
Phospho-Syk (Tyr525/526) Antibody detects transfected Syk protein only when phosphorylated at Tyr525/526 of human Syk or Tyr519/ 520 of mouse Syk. It does not cross-react with other tyrosine-phosphorylated members of the Syk/Zap-70 tyrosine kinase family.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Tyr525/526 of human Syk. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from 293T cells expressing recombinant wild-type and mutant Syk proteins, cotransfected with CD8, using Phospho-Syk (Tyr525/526) Antibody (upper) or Syk Antibody #2712 (lower). (Provided by Dr. Hamid Band, Harvard University, Massachusetts.)
Western Blotting
Dephosphorylation of phosphorylated Wild-type Syk abolishes Phospho-Syk (Tyr525/526) Antibody's recognition of this protein.
Background
Syk is a protein tyrosine kinase that plays an important role in intracellular signal transduction in hematopoietic cells (1-3). Syk interacts with immunoreceptor tyrosine-based activation motifs (ITAMs) located in the cytoplasmic domains of immune receptors (4). It couples the activated immunoreceptors to downstream signaling events that mediate diverse cellular responses, including proliferation, differentiation and phagocytosis (4). There is also evidence of a role for Syk in nonimmune cells, and Syk is a potential tumor suppressor in human breast carcinomas (5). Tyr323 is a negative regulatory phosphorylation site within the SH2-kinase linker region in Syk. Phosphorylation of Tyr323 provides a direct binding site to the TKB domain of Cbl (6,7). Tyrosine 352 of Syk is involved in the association of PLC-γ1 (8). Tyrosines 525 and 526 are located in the activation loop of the Syk kinase domain, and phosphorylation of Tyr525/526 of human Syk (equivalent to the Tyr519/520 of mouse Syk) is essential for Syk function (9).
- Cheng, A.M. and Chan, A.C. (1997) Curr. Opin. Immunol. 9, 528-533.
- Kurosaki, T. et al. (1997) Curr. Opin. Immunol. 9, 309-318.
- Chu, D.H. et al. (1998) Immunol. Rev. 165, 167-180.
- Turner, M. et al. (2000) Immunol. Today 21, 148-154.
- Coopman, P.J. et al. (2000) Nature 406, 742-747.
- Decker, M. et al. (1998) J. Biol. Chem. 273, 8867-8874.
- Rao, N. et al. (2001) EMBO J. 20, 7085-7095.
- Law, C.L. et al. (1996) Mol. Cell. Biol. 16, 1305-1315.
- Zhang, J. et al. (2000) J. Biol. Chem. 275, 35442-35447.
Application References
- Rao, N. et al. (2001) The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation. EMBO J. 20, 7085-7095. This article references the use of Phospho-Syk (Tyr525/526) Antibody in the following applications: Western Blotting
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