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Rabbit Anti-TRIM5 Recombinant Antibody (D6Z8L) (CBMAB-CP2867-LY)

The product is antibody recognizes TRIM5. The antibody D6Z8L immunoassay techniques such as: WB,IP.
See all TRIM5 antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Monkey
Clone
D6Z8L
Antibody Isotype
IgG
Application
WB, IP

Basic Information

Immunogen
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro395 of human TRIM5α protein.
Specificity
Human, Monkey
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
100 µg/ml BSA, 50% glycerol
Preservative
0.02% sodium azide
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
TRIM5 Gene(Protein Coding) Tripartite Motif Containing 5
Introduction
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Dec 2009]
Entrez Gene ID
Human85363
Monkey574288
UniProt ID
HumanQ9C035
MonkeyQ0PF16
Alternative Names
Tripartite Motif Containing 5; RING-Type E3 Ubiquitin Transferase TRIM5; Tripartite Motif Protein TRIM5; RNF88; Tripartite Motif Containing 5 Transcript Variant Kappa; Tripartite Motif Containing 5 Transcript Variant Iota; Tripartite Motif-Containing Protein 5; Tripartite Motif Protein TRIM;
Function
Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811).
Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057).
Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057).
Biological Process
Biological Process activation of innate immune response Source:UniProtKB1 Publication
Biological Process autophagy Source:UniProtKB1 Publication
Biological Process defense response to virus Source:UniProtKB2 Publications
Biological Process innate immune response Source:UniProtKB1 Publication
Biological Process negative regulation of viral entry into host cell Source:UniProtKB1 Publication
Biological Process positive regulation of autophagy Source:GO_Central1 Publication
Biological Process positive regulation of DNA-binding transcription factor activity Source:UniProtKB1 Publication
Biological Process positive regulation of I-kappaB kinase/NF-kappaB signaling Source:UniProtKB1 Publication
Biological Process positive regulation of MAPK cascade Source:UniProtKB1 Publication
Biological Process positive regulation of NF-kappaB transcription factor activity Source:UniProtKB2 Publications
Biological Process protein K63-linked ubiquitination Source:UniProtKB1 Publication
Biological Process protein polyubiquitination Source:GO_Central1 Publication
Biological Process protein ubiquitination Source:GO_Central1 Publication
Biological Process regulation of gene expression Source:GO_Central1 Publication
Biological Process regulation of lipopolysaccharide-mediated signaling pathway Source:UniProtKB1 Publication
Biological Process regulation of protein localization Source:UniProtKB1 Publication
Biological Process regulation of viral entry into host cell Source:GO_Central1 Publication
Biological Process suppression of viral release by host Source:UniProtKB1 Publication
Cellular Location
Cytoplasm
Nucleus
Predominantly localizes in cytoplasmic bodies (PubMed:12878161, PubMed:20357094).
Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27 (By similarity).
In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1 (By similarity).
PTM
Degraded in a proteasome-independent fashion in the absence of viral infection but in a proteasome-dependent fashion following exposure to restriction sensitive virus.
Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. Ubiquitination may not lead to proteasomal degradation.
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For research use only. Not intended for any clinical use.

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