Anti-ARHGEF4 Purified Monoclonal Antibody

ARHGEF4 (Rho guanine nucleotide exchange factor 4), also known as ASEF 1 (adenomatous polyposis coli –; stimulated guanine nucleotide exchange factor 1) is an approximately 80 kDa cytoplasmic protein important for growth factor-mediated regulation of cell morphology and migration. Besides N-terminal adenomatous polyposis coli (APC) -binding region (ABR) it contains Dbl homology (DH), pleckstrin homology (PH) and SH3 domains. The SH3 domain inhibits GEF activity of ARHGEF4 by intramolecular interaction with the DH domain, whereas binding of APC stimulates the GEF activity. Activated ARHGEF4 stimulates the small GTPase Cdc42, which leads to decreased cell-cell adherence and enhanced cell migration.

Recombinant fragment of human ARHGEF4 (amino acids 143-271) . The mouse monoclonal antibody ARHGEF-08 recognizes human intracellular protein ARHGEF4 / ASEF1, approx. 80 kDa guanine nucleotide exchange factor specific for Rac1 and Cdc42. The epitope is located in the rough at the region of SH3 domain.

Expressed at high levels in the brain, skeletal muscle and testis and at low levels in the kidney, lung, small intestine, ovary and prostate. Expression is aberrantly enhanced in most colorectal tumors.

Acts as guanine nucleotide exchange factor (GEF) for RHOA, RAC1 and CDC42 GTPases. Binding of APC may activate RAC1 GEF activity. The APC-ARHGEF4 complex seems to be involved in cell migration as well as in E-cadherin-mediated cell-cell adhesion. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Involved in tumor angiogenesis and may play a role in intestinal adenoma formation and tumor progression.