Phospho-Btk (Y223) Polyclonal Antibody, 100µg, (ATB-P0287)

Description

Background:

The protein encoded by this gene plays a crucial role in B-cell development. Mutations in this gene cause X-linked agammaglobulinemia type 1, which is an immunodeficiency characterized by the failure to produce mature B lymphocytes, and associated with a failure of Ig heavy chain rearrangement. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2013]

Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis.

Product datasheet:

Overview
Product Description	Phospho-Btk (Y223) Polyclonal Antibody, 100µg, (ATB-P0287)
Image
Species Reactivities	Human,Mouse,Rat
Immunogen	Synthesized peptide derived from human Btk around the phosphorylation site of Y223.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. Ibrutinib-naïve chronic lymphocytic leukemia lacks Bruton tyrosine kinase mutations associated with treatment resistance. Famà R, et al. Blood, 2014 Dec 11. PMID 25498455
2. Targeting Bruton’s tyrosine kinase in B cell malignancies. Hendriks RW, et al. Nat Rev Cancer, 2014 Apr. PMID 24658273
3. [Detection of Bruton’s tyrosine kinase gene mutations and clinical analysis of 6 patients with X-linked agammaglobulinemia]. Zhang X, et al. Zhonghua Yi Xue Yi Chuan Xue Za Zhi, 2014 Feb. PMID 24510558
4. A novel Bruton’s tyrosine kinase gene (BTK) invariant splice site mutation in a Malaysian family with X-linked agammaglobulinemia. Chear CT, et al. Asian Pac J Allergy Immunol, 2013 Dec. PMID 24383975
5. Molecular dynamic simulation to explore the molecular basis of Btk-PH domain interaction with Ins(1,3,4,5)P4. Lu D, et al. ScientificWorldJournal, 2013. PMID 24307874 Free PMC Article
6. The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases.
   Vetrie D., Vorechovsky I., Sideras P., Holland J., Davies A., Flinter F., Hammarstroem L., Kinnon C., Levinsky R.J., Bobrow M., Smith C.I.E., Bentley D.R.
   Nature 361:226-233(1993) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BTK-A).
7. Erratum
   Vetrie D., Vorechovsky I., Sideras P., Holland J., Davies A., Flinter F., Hammarstroem L., Kinnon C., Levinsky R.J., Bobrow M., Smith C.I.E., Bentley D.R.
   Nature 364:362-362(1993)
8. Genomic organization and structure of Bruton agammaglobulinemia tyrosine kinase: localization of mutations associated with varied clinical presentations and course in X chromosome-linked agammaglobulinemia.
   Ohta Y., Haire R.N., Litman R.T., Fu S.M., Nelson R.P., Kratz J., Kornfeld S.J., la Morena M., Good R.A., Litman G.W.
   Proc. Natl. Acad. Sci. U.S.A. 91:9062-9066(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
9. The genomic structure of human BTK, the defective gene in X-linked agammaglobulinemia.
   Rohrer J., Parolini O., Belmont J.W., Conley M.E.
   Immunogenetics 40:319-324(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
10. Genomic organization of the Btk gene and exon scanning for mutations in patients with X-linked agammaglobulinemia.
    Hagemann T.L., Chen Y., Rosen F.S., Kwan S.-P.
    Hum. Mol. Genet. 3:1743-1749(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLA SER-334; ARG-506; GLN-520; TRP-562 AND LYS-630.