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

q9nry4

Human,Mouse,Rat

WB,IHC

WB 1:500-1:1000
IHC 1:50-1:200

~ 172 kDa

Rabbit

This antibody detects endogenous levels of GRF-1 protein only when phosphorylated at Tyr1105.

Synthetic phosphopeptide derived from human GRF-1 around the phosphorylation site of Tyrosine 1105.

Polyclonal

Rabbit IgG

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

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.