Spleen tyrosine Kinase (SYK) (C-Term), (pTyr526), (pTyr527) antibody

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Antigen
  • p72-Syk
  • Sykb
  • p72syk
  • Tyrosine-protein kinase SYK
  • spleen tyrosine kinase
  • ksyk
  • SYK
  • Syk
Alternatives
anti-Human Spleen tyrosine Kinase antibody for Immunofluorescence (fixed cells)
Epitope
C-Term, pTyr526, pTyr527
50
31
24
24
20
16
15
13
12
12
11
10
9
9
9
9
8
7
6
5
5
4
4
4
3
3
3
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine)
360
160
133
13
11
9
8
8
4
3
1
1
Host
Rabbit
262
90
19
Clonality
Polyclonal
Conjugate
Un-conjugated
14
11
10
8
6
6
3
2
2
2
2
2
2
2
2
2
2
Application
Immunohistochemistry (IHC)
294
136
115
74
73
45
27
23
14
8
4
4
3
3
2
2
1
1
1
1
1
Options
Supplier
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human SYK (Tyrosine-protein kinase SYK)
Alternative Name SYK (SYK Antibody Abstract)
Background 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.
Research Area Signaling
Pathways Fc-epsilon Receptor Signaling Pathway, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Thromboxane A2 Receptor Signaling
Restrictions For Research Use only
Background publications Rikova, Guo, Zeng, Possemato, Yu, Haack, Nardone, Lee, Reeves, Li, Hu, Tan, Stokes, Sullivan, Mitchell, Wetzel, Macneill, Ren, Yuan, Bakalarski, Villen, Kornhauser, Smith, Li, Zhou, Gygi, Gu et al.: "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. ..." in: Cell, Vol. 131, Issue 6, pp. 1190-203, 2007 (PubMed).

Product cited in: 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).

Tang, Sawasdikosol, Chang, Burakoff: "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).

Deckert, Elly, Altman, Liu: "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).

Yagi, Suzuki, Hasegawa, Okumura, Ra: "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, Draves, Chan, Weiss, Edelhoff, Disteche, Clark: "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).