RIAM polyclonal antibody; host Rabbit; reactivity Human, Rat, Mouse
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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.,
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species / reactivity | WB | ELISA |
|---|---|---|
| Human,Rat,Mouse |
This product is manufactured by Reed Biotech and sold through ABMIUM without relabelling.
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