Recombinant full-length human protein was used as the immunogen for the Serum Response Factor antibody.
Serum response factor (SRF) is a transcription factor that binds the serum response element (SRE), a sequence that mediates the transient response of many cellular genes to growth stimulation. SRF-binding sites are also constitutive promotor elements in many muscle-specific promotors. At the c-Fos SRE, formation of a ternary complex containing SRF and its accessory protein p62TCF appears to be important for signal transduction. Two related Ets domain proteins, Elk-1 and SRF accessory protein-1 (SAP-1), have DNA binding properties identical to that of p62TCF. Elk-1 and SAP-1 contain two homologous regions of which the two amino-terminal regions, the Ets domain (box A) and the B box, mediate ternary complex formation with SRF. The third homologous region, the C box located toward the C-terminus of the proteins, contains conserved consensus phosphorylation sites for MAP kinases.
