Recombinant Rabbit monoclonal primary
Phospho-Stat5 (Y694) Recombinant Rabbit Monoclonal Antibody [SC05-31] (ET1610-48)
Synthetic phospho-peptide corresponding to residues surrounding tyr694 of human stat5a.
Mouse liver tissue lysates, human breast carcinoma tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
MGF antibody; Signal transducer and activator of transcription 5A antibody; Signal Transducer and Activator of Transcription 5B antibody; STA5A_HUMAN antibody; STAT 5A antibody; STAT 5B antibody; STAT5 antibody; STAT5A antibody; STAT5B antibody; Transcription factor STAT5A antibody; Transcription factor STAT5B antibody
Belongs to the transcription factor STAT family.
Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (By similarity). Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Tyrosine phosphorylation is required for DNA-binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity (By similarity). Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 at Tyr-694.; ISGylated.
Stat5 (Signal Transducers and Activators of Transcription 5) is important in regulating T cell functions involving the receptors for Interleukin-2 (IL-2). IL-2 stimulates the rapid phosphorylation of both serine and tyrosine residues of Stat5a and Stat5b in human T lymphocytes and in several IL-2-responsive lymphocytic cell lines. IL-2 differentially induces serine phosphorylation of Stat5a and Stat5b on Ser726 and Ser731, respectively. Stat5b is preferentially phosphorylated and displays more protracted serine phosphorylation kinetics than Stat5a. Both the acid-rich region and the COOH terminus of IL-2Rb can independently mediate IL-2-induced Stat 5a/b serine phosphorylation, suggesting that Stat5a/b serine phosphorylation occurs at a postreceptor level. Stat5a is phosphorylated on Tyr694 in a prolactin-sensitive manner, whereas serine phosphorylation is constitutive. Activation of Stat5 by IL-2 may help govern the biological effects of IL-2 during the immune response.