Aqueous buffered solution containing BSA and ≤0.09 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Informationen zur Lagerung
The antibody was conjugated with R-PE under optimum conditions, and unconjugated antibody and free PE were removed. Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.
Marshall, Niiro, Yun, Clark: "Regulation of B-cell activation and differentiation by the phosphatidylinositol 3-kinase and phospholipase Cgamma pathway." in: Immunological reviews, Vol. 176, pp. 30-46, (2001) (PubMed).
Rawlings, Scharenberg, Park, Wahl, Lin, Kato, Fluckiger, Witte, Kinet: "Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases." in: Science (New York, N.Y.), Vol. 271, Issue 5250, pp. 822-5, (1996) (PubMed).
Mahajan, Fargnoli, Burkhardt, Kut, Saouaf, Bolen: "Src family protein tyrosine kinases induce autoactivation of Bruton's tyrosine kinase." in: Molecular and cellular biology, Vol. 15, Issue 10, pp. 5304-11, (1995) (PubMed).
Bruton's tyrosine kinase (Btk) is a nonreceptor tyrosine kinase whose function is critical for proper B cell development and signaling. It is a member of the Tec family of kinases which includes Tec and Itk. This family is similar to the src family of tyrosine kinases. However, Tec family members lack the N-terminal myristylation site and the regulatory C-terminal tyrosine that are found in src proteins. In addition to an N-terminal pleckstrin homology (PH) domain, the Tec proteins contain Src homology domains 2 and 3 (SH2 and SH3) and a stretch of 60-80 amino acids between the PH and SH3 domains termed the Tec homology domain. The activity of Btk is regulated by Src-mediated phosphorylation of the kinase domain at tyrosine 551. This event induces Btk kinase activity and subsequent autophosphorylation at tyrosine 223 in the SH3 domain. Phosphorylated Btk then associates with the cell membrane via the interaction of the PH domain with phosphatidylinositol 3, 4, 5-triphosphate. The PH domain is essential for proper activation and function of Btk. A mutation in the PH domain results in Xid, murine X-linked immunodeficiency, and human X-linked agammaglobulinemia.