GRF-1 (phospho-Y1105) polyclonal antibody

GRF-1 (glucocorticoid receptor DNA-binding factor 1), also known as p190RhoGAP or simply p190, is a transcriptional regulator which binds to the promoter region of the glucocorticoid receptor gene and represses its expression. By repressing GR expression, GRF-1 acts to down-regulate Rho signaling, thereby mediating both actin cytoskeletal rearrangements and cell cycle events. Through its GAP domain, GRF-1 is thought to affect cytokinesis by regulating Rho activity; a regulation that is controlled by the ubiquination of the GTP binding region and subsequent degradation of GRF-1. Additionally, GRF-1 plays an important role in oligodendrocyte differentiation, a process that is absent in malignant glioma tumors, implicating GRF-1 as a possible tumor suppressor. GRF-1 expression is regulated by glucocorticoids and the expressed protein exists as two isoforms produced by alternative splicing events.

Rho GTPase-activating protein 35; Glucocorticoid receptor DNA-binding factor 1; Glucocorticoid receptor repression factor 1; GRF-1; Rho GAP p190A; p190-A; ARHGAP35; GRF1; GRLF1; KIAA1722

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 p-GRF-1 (Y1105) pAb at 1:500 dilution Lane1:The Heart tissue lysate of Rat (40ug) Lane2:K562 whole cell lysate (40ug) Lane3:Jurkat whole cell lysate (40ug) Lane4:The Blood tissue lysate of Mouse (40ug) Lane5:H1792 whole cell lysate (40ug) Lane6:HEK293T whole cell lysate (40ug) Lane7:SP2/0 whole cell lysate (40ug)