Phospho-SRC-3 (Thr24) Antibody detects endogenous levels of SRC-3 protein only when phosphorylated on Thr24. This antibody does not cross-react with other family members.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to sequence surrounding Thr24 of the human SRC-3 protein. Antibodies are purified by protein A and peptide affinity chromatography.Background
There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2) and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). The SRC family members all share significant structural homology and function in a similar fashion to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as STAT3, NF-κB, E2F1 and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines and growth factors and involve multiple kinase signaling pathways (9-11). All three SRC family members are associated with increased activity of nuclear receptors in breast, prostate and ovarian carcinomas. In addition, SRC-3 is frequently amplified or over-expressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).
Phosphorylation of Thr24 of SRC-3 proteins can be induced by stimulation with EGF. Phosphorylated SRC-3 translocates from the cytoplasm to the nucleus where it interacts with other transcription factors and steroid hormone receptors and regulates gene expression (15).