Anti-Src

0.5mg/ml if reconstituted with 0.2ml sterile DI water. The nuclear receptor coactivator 1 (NCOA1), also known as Src1, is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. Src is recruited to DNA promotion sites by ligand-activated nuclear receptors. It in turn acylates histones, which makes downsteam DNA more accessible to transcription. Hence, it assists nuclear receptors in the upregulation of DNA expression. It has been found that the protein can enhance the transcriptional activity of ligand-bound PGR but does not alter the basal activity of the target promoter. It also enhances estrogen receptor, glucocorticoid receptor, thyroid hormone receptor, and retinoid X receptor transcriptional activities through their cognate DNA response elements in the presence of hormone. Additionally, Src may play a role as a bridging molecule between nuclear hormone receptors and general transcription factors. Protein function: Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4, the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. [The UniProt Consortium]