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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2.
Application Dilute:
WB: 1:500~1:1000
Application Notes:
RASGRF1(Phospho-S916) polyclonal antibody detects endogenous levels of RASGRF1 protein only when phosphorylated at Ser916.
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