Render Target: SSR
Render Timestamp: 2024-11-14T23:08:09.150Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-30 01:54:05.107
Product last modified at: 2024-10-30T18:30:09.873Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

TRIM5α (D6Z8L) Rabbit mAb #14326

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 56
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    TRIM5α (D6Z8L) Rabbit mAb recognizes endogenous levels of total TRIM5α protein. This antibody does not react with human TRIM5β and is not predicted to react with other human TRIM5 isoforms based on the location of the antigen.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro395 of human TRIM5α protein.

    Background

    TRIM5α is a retroviral restriction factor that was originally identified as an HIV restriction factor in Old World monkeys (1). The restriction specificity of TRIM5α varies between species (2). Human TRIM5α only weakly restricts HIV, but efficiently restricts N-tropic murine leukemia virus (N-MLV) (1-3). TRIM5α is composed of a tripartite motif containing RING, B-box 2, and coiled-coil domains, and a B30.2/SPRY domain (4). A 13 amino acid stretch of the B30.2/SPRY domain containing multiple positively charged residues was found to be essential for viral restriction and responsible for variations across species in restriction specificity (4,5). TRIM5α blocks viral infection by interacting with the incoming viral capsid and promoting its premature disassembly (1,6,7). In addition, TRIM5α, together with UBC13-UEV1A, promotes innate immune signaling by catalyzing the synthesis of K63-linked ubiquitin chains that activate TAK1, AP-1, and NF-κB (8).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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