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RICH1 is a GTPase-activating protein (GAP). Additionally we are shipping rho GTPase Activating Protein 17 Antibodies (38) and many more products for this protein.
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In vitro analysis demonstrated that ARHGAP17 overexpression inhibited cell growth and invasion of HCT-8 and HCT-116 cells.
show that ARHGAP17 binds to the actin-regulating CIP4 protein in platelets and that Ser (show SIGLEC1 Proteins)-702 phosphorylation interferes with this interaction
Rich1 negatively regulates the epithelial cell cycle, proliferation and adhesion by CDC42/RAC1-PAK1-Erk1/2 pathway.
We propose that Rich1 and Amot (show AMOT Proteins) maintain TJ integrity by the coordinate regulation of Cdc42 (show CDC42 Proteins) and by linking specific components of the TJ to intracellular protein (show CKAP2 Proteins) trafficking.
Arhgap17 regulates mucosal and epithelial barrier function in the mouse colon.
The phosphorylation of Nadrin leads to tightly regulated Rho activation that was found to be Nadrin isoform- and (Rho) target-specific.
NADRIN is associated with the ERM (show ETV5 Proteins) protein complex, where it inactivates RhoA (show RHOA Proteins) and leads to the morphological differentiation of astrocytes.
A critical role for Nadrin in the regulation of RhoA, Cdc42 and Rac1 in platelets and thus for platelet adhesion and aggregation.
RICH1 is a GTPase-activating protein (GAP). GAPs stimulate the intrinsic GTP hydrolysis of small G proteins, such as RHOA (MIM 165390), RAC1 (MIM 602048), and CDC42 (MIM 116952).
Rho GTPase activating protein 17
, rho GTPase-activating protein 17-like
, RhoGAP interacting with CIP4 homologs 1
, neuron-associated developmentally regulated protein
, rho GTPase-activating protein 17
, rho-type GTPase-activating protein 17
, rhoGAP interacting with CIP4 homologs protein 1
, WW domain-binding protein 15
, neuron-associated developmentally-regulated protein
, neuron-specific GTPase activating protein
, neuron-specific GTPase-activating protein