RIAM rabbit pAb - ES6660

RIAM rabbit pAb

Sizes: 50μL, 100μL

Catalogue Numbers: ES6660-50, ES6660-100

Citations, Manuals and MSDS Available upon request.

Background: 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.,

Alternate Name: APBB1IP; PREL1; RARP1; RIAM; Amyloid beta A4 precursor protein-binding family B member 1-interacting protein; APBB1-interacting protein 1; Proline-rich EVH1 ligand 1; PREL-1; Proline-rich protein 73; Rap1-GTP-interacting adapter molecule; R

Source: Rabbit

Applications: WB; IHC

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

Reactivity: Human; Rat; Mouse;

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

Storage and Stability: -20°C/1 year

Clonality: Polyclonal

Isotype: IgG

Concentration: 1 mg/ml

Observed Band (KD): 73kD

Human Gene ID: 54518

Human SWISS Prot NO: Q7Z5R6

Subcellular Location: Cell membrane; Peripheral membrane protein. Cell projection, lamellipodium. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. 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 (By similarity).

Research Use Only