Human;Rat;Mouse;

WB;IHC

Synthesized peptide derived from RIAM . at AA range: 430-510

RIAM Polyclonal Antibody detects endogenous levels of RIAM protein.

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

WB 1:500-2000;IHC-p 1:50-300

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

1 mg/ml

domain:The two Pro-rich regions are required for the suppression of AP1 transcription activity.,function:Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.,induction:Induced by all-trans-retinoic acid.,similarity:Belongs to the MRL family.,similarity:Contains 1 PH domain.,similarity:Contains 1 Ras-associating domain.,subcellular location:Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases.,subunit:Interacts, through the N-terminal Pro-rich region, with the WW domain of APBB1. Interacts with RAP1A, PFN1, VASP and ENAH.,tissue specificity:Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes.,

domain:The two Pro-rich regions are required for the suppression of AP1 transcription activity.,function:Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.,induction:Induced by all-trans-retinoic acid.,similarity:Belongs to the MRL family.,similarity:Contains 1 PH domain.,similarity:Contains 1 Ras-associating domain.,subcellular location:Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases.,subunit:Interacts, through the N-terminal Pro-rich region, with the WW d

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