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|Background:||STATs (signal transducers and activators of transcription) were originally identified as two novel DNA-binding proteins (STAT1 and STAT2) which were found to play central roles in interferon IFNa- and IFNg-regulated gene expression(reviewed in 2). Following the identification of these first two family members, five additional mammalian STAT proteins have been cloned, and characterized including: STAT3, STAT4, STAT5a, STAT5b, and STAT6(1,2). All STAT proteins share several conserved structural and functional domains which are illustrated below(1,2): YN-Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦Â¦ -C 1 2 3 4 5 6 (1) conserved amino terminal domain (2) DNA binding domain (3) SH3-like region (4) conserved SH2 domain responsible for recruitment to the receptor interaction with JAKs STAT dimerization (5) conserved tyrosine residue whose phosphorylation is required for dimerization and DNA binding (6) carboxy terminal activation domain In unstimulated cells, STAT proteins exist largely in the cytoplasm as latent transcription factors. In response to treatment of target cells with cytokines or in some cases growth factors, STATs undergo tyrosine phosphorylation, homo-or heterodimerization, nuclear translocation, and DNA binding which results in transcriptional activation of distinct target genes(1,2). At least one and oftentimes several STAT proteins are activated in response to all cytokines which utilize cytokine receptor superfamily members. Nevertheless, a striking specificity of specific STAT activation is seen in response to individual cytokines(1). STAT6 (IL-4 STAT) was originally purified and cloned from Il-4 stimulated human myeloid cells.(3) IL-4 rapidly alters the pattern of gene expression in cells expressing the IL-4 receptor, and inducible tyrosine phosphorylation of the STAT6 protein requires the membrane-distal region of the IL-4 receptor alpha-chain.(3) Perhaps not surprisingly, STAT6-null mice (STAT6-/-) were found to be deficient in IL-4-mediated functions including Th2 helper T-cell differentiation, expression of cell surface markers, T-cell proliferation, immunoglobulin class switching to IgE, and partial loss of IL-4 mediated proliferation.(5,6) STAT6 mRNA has been detected in various tissues including: peripheral blood lymphocytes, colon, intestine, ovary, prostate, thymus, spleen, kidney, liver, lung and placenta.(4) STAT6 migrates as a 100 kDa protein when analyzed by SDS-PAGE and shares the greatest degree of amino acid sequence homology with the STAT5 protein.(4) The preferred STAT6 DNA consensus binding site has been identified as TTCC(A>T,N)GGAA.(2)|
|Regulatory Statement:||For Research Use Only. Not for use in diagnostic procedures.|
|Product Type:||Primary Antibody|
Applications: WB, ELISA
There are no references for STAT6 Monoclonal Antibody at this time.