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Human Polyclonal AGAP3 Primary Antibody for ELISA - ABIN547167
Surks, Richards, Mendelsohn: Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA. in The Journal of biological chemistry 2003
AGAP3 expression was significantly increased in colorectal cancer (CRC)and colorectal adenoma compared to normal tissue. CRAG overexpression up-regulated c-Jun expression, and significantly increased cell proliferation and colony formation capability. AGAP3 expression did not have a concordant association with patient prognosis among datasets
AGAP3 is an essential signaling component of the NMDA receptor complex that links NMDA receptor activation to AMPA receptor trafficking.
M-RIP can assemble a complex containing both RhoA and Myosin phosphatase myosin binding subunit, suggesting that M-RIP may play a role in myosin phosphatase regulation by RhoA
CRAG enhances the cell survival signal against the accumulation of unfolded proteins, including polyQ, through not only proteasome activation, but also the activation of c-Fos-dependent AP-1.
We propose that CRAG is a modulator of promyelocytic leukemia protein function and dynamics in reactive oxygen species signaling and is protectively involved in the pathogenesis of polyglutamine diseases.
GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway.
ArfGAP with GTPase domain, ankyrin repeat and PH domain 3
, centaurin, gamma 3
, arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3-like
, CRAM-associated GTPase
, CRMP (collapsin response mediator protein) associated
, MR1-interacting protein
, arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3