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Details for Product No. ABIN968375

Bruton Agammaglobulinemia tyrosine Kinase (BTK) (N-Term), (AA 2-172) antibody

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Antigen
Synonyms AI528679, xid, AGMX1, AT, ATK, BPK, IMD1, PSCTK1, XLA, BTK, atk, bpk, xla, imd1, agmx1, psctk1
Epitope
»Alternatives N-Term, AA 2-172
Reactivity
»Alternatives Human
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Conjugate
»Alternatives Un-conjugated
Application
»Alternatives Western Blotting (WB), Immunofluorescence (IF)
Pubmed 5 references available
Catalog no. ABIN968375
Quantity 150 µg
Price
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Immunogen Human Btk Recombinant Protein
Clone FB11
Isotype IgG2a
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Purity Purified
Alternative Name Btk
Background 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.
Molecular Weight 77 kDa
Comment

Related Products: ABIN968584, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Storage -20 °C
Product cited in: Aoki, Isselbacher, Pillai: "Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 22, pp. 10606-9, 1994 (PubMed).

Yang, Malek, Desiderio: "An SH3-binding site conserved in Bruton's tyrosine kinase and related tyrosine kinases mediates specific protein interactions in vitro and in vivo." in: The Journal of biological chemistry, Vol. 270, Issue 35, pp. 20832-40, 1995 (PubMed).

Sideras, Müller, Shiels et al.: "Genomic organization of mouse and human Bruton's agammaglobulinemia tyrosine kinase (Btk) loci." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 153, Issue 12, pp. 5607-17, 1995 (PubMed).

Vetrie, Vorechovský, Sideras et al.: "The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases." in: Nature, Vol. 361, Issue 6409, pp. 226-33, 1993 (PubMed).

Shahan, Sorenson, Simpson et al.: "Tyrosine kinase activation in response to fungal spores is primarily dependent on endogenous reactive oxygen production in macrophages." in: The Journal of biological chemistry, Vol. 275, Issue 14, pp. 10175-81, 2000 (PubMed).

Alternatives for antigen "Bruton Agammaglobulinemia tyrosine Kinase (BTK)", type "Antibodies"
Hosts (104), (37)
Reactivities (142), (68), (62), (36), (36), (24), (6), (1)
Applications (105), (54), (40), (36), (31), (29), (17), (16), (6), (1)
Conjugates (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4)
Epitopes (20), (19), (14), (12), (4), (3), (2), (2), (1), (1), (1), (1), (1)
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