ARHGDIA / Unconjugated / G8-C3

Product Details

Description	Members of the Ras superfamily of small GTP-binding proteins are critical mediators of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion. The counter-conversion of the active GTP-bound form of these proteins to their inactive GDP-bound form is influenced by two types of regulatory proteins: those that alter the intrinsic GTPase activity of the GTP-binding proteins and those that alter the rate of GDP/GTP exchange. Guanine nucleotide-releasing factors (GRFs) increase the GDP dissociation rate, while GDP-dissociation inhibitors (GDIs) decrease the dissociation rate. Rho GDIα, also known as ARHGDIA or GDIA1, is a 204 amino acid member of the Rho GDI family of proteins. Localized to the cytoplasm, Rho GDIα inhibits the dissociation of GDP from Rho proteins, thereby preventing GTP from binding to and subsequently activating Rho proteins. In humans, Rho GDIα can be phosphorylated at Ser 101 by p21-activated kinase (αPAK), an event that inhibits Rho GDIα activity and may result in positive feedback regulation of certain Rho GDIα target proteins.
Conjugate	Unconjugated
Clone	G8-C3
Target Species	Human, Monkey, Mouse
Applications	FC, ICC, WB
Supplier	HuaBio
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About ARHGDIA
This gene encodes a protein that plays a key role in the regulation of signaling through Rho GTPases. The encoded protein inhibits the disassociation of Rho family members from GDP (guanine diphosphate), thereby maintaining these factors in an inactive state. Activity of this protein is important in a variety of cellular processes, and expression of this gene may be altered in tumors. Mutations in this gene have been found in individuals with nephrotic syndrome, type 8. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014]

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