Btk (Bruton's tyrosine kinase) is a member of the Tec family of protein tyrosine kinases (PTKs) and plays a modulatory role in many cellular processes, such as proliferation, development, differentiation, survival, and apoptosis. The Tec kinases are the second largest family of non-receptor tyrosine kinases and include Tec, Btk, Bmx, Itk, and TXK/Rlk. Mutations of Btk gene cause a primary immunodeficiency disease in humans, X-linked aγglobulinemia (XLA) which is characterized by a lack of circulating B lymphocytes and an absence of immunoglobulins as a result of defects in B cell maturation and function. Btk is found in all hematopoietic cells, with the exception of T lymphocytes and plasma cells. Btk contains amino-terminal PH (pleckstrin homology) domain which binds phosphatidylinositol (3,4,5)-trisphosphate (PIP3) helping membrane translocation upon PI3 kinase activation. The Tec kinases have similar structure of N-terminal PH domains followed by Tec homology (TH), Src homology 3 (SH3), Src homology 2 (SH2), and kinase domains. Autophosphorylation of Tyr223 in SH3 domain is necessary for full activation of Btk. Various binding proteins have been reported to interact with different domains of Btk.

Western Blot: 0.5ug/ml; Immunohistochemistry: Paraffin-embedded sections;

Type: Primary
Antigen: IBTK (inhibitor of Bruton agammaglobulinemia tyrosine kinase)
Clonality: Monoclonal
Clone: 1A1
Conjugation: Unconjugated
Epitope:
Host: Mouse
Isotype: IgG1 Kappa
Reactivity: Human