Anti-RIAM Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, IHC-F, ICC |
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Primary Accession | Q7Z5R6 |
Host | Rabbit |
Reactivity | Human, Rat |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Amyloid beta A4 precursor protein-binding family B member 1-interacting protein(APBB1IP) detection. Tested with WB, IHC-P, IHC-F, ICC in Human;Rat. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 54518 |
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Other Names | 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, RIAM, Retinoic acid-responsive proline-rich protein 1, RARP-1, APBB1IP, PREL1, RARP1, RIAM |
Calculated MW | 73183 MW KDa |
Application Details | Immunocytochemistry , 0.5-1 µg/ml, Human, Rat Immunohistochemistry(Frozen Section), 0.5-1 µg/ml, Rat, Human Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Rat, By Heat Western blot, 0.1-0.5 µg/ml, Human, Rat |
Subcellular Localization | 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). . |
Tissue Specificity | Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes. . |
Protein Name | Amyloid beta A4 precursor protein-binding family B member 1-interacting protein |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
Immunogen | A synthetic peptide corresponding to a sequence at the C-terminus of human APBB1IP(647-666aa EQDFMSDLMKALQKKRGNVS), different from the related rat sequence by one amino acid, and from the related mouse sequence by two amino acids. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Sequence Similarities | Belongs to the MRL family. |
Name | APBB1IP |
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Synonyms | PREL1, RARP1, RIAM |
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. |
Cellular Location | Cell membrane; Peripheral membrane protein. Cell projection, lamellipodium Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Note=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). |
Tissue Location | Widely expressed with high expression in thymus, spleen, lymph node, bone marrow and peripheral leukocytes |
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Provided below are standard protocols that you may find useful for product applications.
Background
APBB1IP(APBB1-Interacting Protein), also called RIAM or RARP1, is a protein that in humans is encoded by the APBB1IP gene. By genomic sequence analysis, Lafuente et al.(2004) mapped the RIAM gene to chromosome 10p12.1. Using promoter-reporter gene assays, Inagaki et al.(2003) found that RARP1 suppressed transcription from AP1 and SRE sites, but not CRE sites, in all cell lines examined. The proline-rich regions of RARP1 suppressed AP1 transactivation. Lafuente et al.(2004) found that RIAM interacted with profilin and VASP, molecules that regulate actin dynamics, as well as with RAP1-GTP.
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