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.
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 IHC: 1:50~1:200
Application Notes:
p-GRF-1 (Y1105) polyclonal antibody detects endogenous levels of GRF-1 protein only when phosphorylated at Tyr1105.
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