RASGRF1 (Phospho-S916) polyclonal antibody

A critical step in signal transduction responses to stimulation of cell surface receptors by their ligands involves the accumulation of Ras proteins in their active GTP-bound state. To reach their active GTP-bound state, Ras proteins must first release bound GDP, a rate-limiting step mediated by a guanine nucleotide releasing factor (GRF) . The mammalian Ras p21 GRF protein has been designated Ras-GRF p140. Ras-GRF accelerates release of GDP from H- and N-Ras p21 protein in vitro, but not from the related Ral A or Cdc42Hs GTP-binding proteins. Of interest, a region mapping within the amino terminal domain of Ras-GRF is similar to both the human breakpoint cluster protein, Bcr, and the Dbl proto-oncogene product, a guanine nucleotide-releasing factor for CDC42Hs. Ras-GRF2 p135 has also been identified. Ras-GRF2 p135 is highly homologous to Ras-GRF1 p140 except in the region between the REM and CDC25 domains and appears to function similarly to Ras-GRF1 p140.

Ras-specific guanine nucleotide-releasing factor 1; Ras-GRF1; Guanine nucleotide-releasing protein; GNRP; Ras-specific nucleotide exchange factor CDC25; RASGRF1; CDC25; GNRP; GRF1

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of RASGRF1 (Phospho-S916) polyclonal antibody at 1:500 dilution Lane1:U-87MG whole cell lysate (40ug) Lane2:H1792 whole cell lysate (40ug) Lane3:Panc1 whole cell lysate (40ug) Lane4:A549 whole cell lysate (40ug)