B Cell Signaling Antibody Sampler Kit II #72159
Product Information
Kit Usage Information
Protocols
- 2710: Western Blotting, Immunoprecipitation (Agarose), Immunofluorescence, Flow
- 3571: Western Blotting, Immunoprecipitation (Magnetic)
- 3601: Western Blotting, Immunoprecipitation (Magnetic)
- 5173: Western Blotting, Immunoprecipitation (Magnetic), Immunofluorescence, Flow
- 7074: Western Blotting
- 8547: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Leica® Bond™), Immunohistochemistry (Paraffin), Flow
- 13198: Western Blotting, Immunoprecipitation (Magnetic), Immunohistochemistry (Paraffin), Immunofluorescence, Flow
- 13333: Western Blotting, Immunohistochemistry (Paraffin)
- 87457: Western Blotting, Immunoprecipitation (Magnetic)
- 90176: Western Blotting, Immunoprecipitation (Agarose), Immunohistochemistry (Leica® Bond™), Immunohistochemistry (Paraffin), Flow
Product Description
Specificity / Sensitivity
Source / Purification
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 that Syk plays a role in nonimmune cells; Syk is a potential tumor suppressor in human breast carcinomas (5). Tyrosine 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 (6).
Lyn, one of the Src family members, is predominantly expressed in hematopoietic cells (7). Two tyrosine residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family. Autophosphorylation of Tyr396 (equivalent to Tyr416 of Src), located in the catalytic domain, correlates with enzyme activation. Csk-mediated phosphorylation of the carboxy-terminal Tyr507 (equivalent to Tyr527 of Src) inactivates the kinase. Tyrosine phosphorylation and activation of Lyn occurs upon association with cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (8-10).
Bruton's tyrosine kinase (Btk) is a member of the Btk/Tec family of cytoplasmic tyrosine kinases. Btk plays an important role in B cell development (11,12). Activation of B cells by various ligands is accompanied by Btk membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate (13-15). The membrane-located Btk is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation (16,17).
CD19 is a 95 kDa coreceptor that amplifies the signaling cascade in B cells (18). On the B cell surface, CD19 associates with CD21, CD81, and Leu-13 to exert its function. The cytoplasmic tail of CD19 has nine conserved tyrosine residues playing critical roles in CD19-mediated function by coupling signaling molecules to the receptor (18). After BCR or CD19 ligation, Tyr531 and Tyr500 of CD19 are progressively phosphorylated. This phosphorylation enables the coupling of PI3 kinase and Src family tyrosine kinase to CD19 and activates the PI3K and Src signaling pathways (19,20).
B cell linker protein (BLNK), also known as SLP-65 or BASH, is an adaptor molecule that plays key roles in B cell activation and B cell antigen receptor (BCR) engagement. BLNK acts at the interface between BCR-associated Syk and downstream signaling cascades.
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