Signal Transducer and Activator of Transcription 5A (STAT5A) (pTyr694) antibody
|Synonyms||MGF, STAT5, AA959963, Stat5, STATA5, STAT5A/MGF, STAT5A|
Alternatives Western Blotting (WB)
|5 references available|
|Quantity||150 µg (250 µg/ml) (Variants)|
|Price||Product not available in this region.|
|Immunogen||Phosphorylated Sheep Stat5 Peptide|
Stat (Signal transducer and activators of transcription) proteins are critical mediators of the biologic activity of cytokines, including interleukins, interferons, erythropoietin, and growth factors. Ligand-receptor interaction leads to activation of constitutively associated JAK family kinases and subsequent recruitment/activation of Stat proteins by tyrosine phosphorylation. Active Stat proteins then move to the nucleus to promote transcription of cytokine-inducible genes. Seven Stat proteins have been cloned, each of which is differentially expressed and/or activated in a cytokine-specific and cell type-specific manner. Stat5 has been characterized and shown to be encoded by two separate genes, Stat5a and Stat5b that share over 90% identity at the amino acid level. Stat5a has been shown to be involved in lactogenesis and mammary development, while Stat5b has been shown to be involved in growth hormone signaling and to play a role in liver gene expression. Both Stat5a and Stat5b share similarities, both are involved in IL-2 induced peripheral T cell proliferation. The peptide hormone, prolactin, binds to the prolactin receptor (PRLR) to initiate the lactogenic response. There are at least three forms of PRLR, however, only the long form is able to activate the 92-kDa Stat5 protein by inducing phosphorylation at Y694. Once phosphorylated, Stat5 becomes an essential transcription factor which binds to the beta-casein gene promoter. The presence of an SH2 domain within Stat5 suggests that it may directly interact with protein tyrosine kinases (PTKs) such as JAK2.
The 47 monoclonal antibody recognizes the phosphorylated Y694 of Stat5a. The homologous phosphorylation site in Stat5b is Y699.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||92 kDa|
Related Products: ABIN968534, ABIN967389, ABIN967810
|Application Notes||Immunofluorescent staining and flow cytometry: Conjugated formats of this antibody are available and recommended.|
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20° C.|
|Research Area||Signaling, Receptors, Inflammation|
|Restrictions||For Research Use only|
Wakao, Gouilleux, Groner: "Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response." in: The EMBO journal, Vol. 13, Issue 9, pp. 2182-91, 1994 (PubMed).
Gouilleux, Pallard, Dusanter-Fourt et al.: "Prolactin, growth hormone, erythropoietin and granulocyte-macrophage colony stimulating factor induce MGF-Stat5 DNA binding activity." in: The EMBO journal, Vol. 14, Issue 9, pp. 2005-13, 1995 (PubMed).
Gouilleux, Wakao, Mundt et al.: "Prolactin induces phosphorylation of Tyr694 of Stat5 (MGF), a prerequisite for DNA binding and induction of transcription." in: The EMBO journal, Vol. 13, Issue 18, pp. 4361-9, 1994 (PubMed).
Park, Lee, Frank et al.: "Caveolin-1-deficient mice show accelerated mammary gland development during pregnancy, premature lactation, and hyperactivation of the Jak-2/STAT5a signaling cascade." in: Molecular biology of the cell, Vol. 13, Issue 10, pp. 3416-30, 2002 (PubMed).
Williams, Cheung, Park et al.: "Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice." in: Molecular biology of the cell, Vol. 14, Issue 3, pp. 1027-42, 2003 (PubMed).