Product Pathways - Nuclear Receptor Signaling
Phospho-SRC-3 (Thr24) Antibody #2979
Reactivity Key: H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
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.
Western blot analysis of cell extracts from MCF-7 cells, untreated or stimulated with heregulin, using Phospho-SRC-3 (Thr24) Antibody (upper and middle) or SRC-3 (5E11) Rabbit mAb #2126 (lower). The middle blot was treated with calf intestinal phosphatase (CIP) before antibody probing.
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). All SRC family members share significant structural homology and function 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). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed 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).
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For Research Use Only. Not For Use In Diagnostic Procedures.