TRIM5 Antibody
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Description
Introduction to TRIM5 Antibody
TRIM5 antibodies are immunological tools designed to detect and study TRIM5 (tripartite motif-containing 5), a protein critical for antiviral defense and innate immune signaling . These antibodies enable researchers to investigate TRIM5's expression, localization, and interaction partners in cellular and disease contexts. TRIM5 exists in multiple isoforms (α, β, γ, δ, ε, ι) with molecular weights ranging from 29 kDa to 56 kDa, necessitating antibodies validated for specificity against distinct isoforms or shared epitopes .
Role in Antiviral Defense
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Capsid Lattice Recognition: TRIM5 antibodies have confirmed the protein’s ability to form hexagonal nets on HIV-1 capsids, a mechanism critical for viral restriction .
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Innate Immune Activation: Studies using TRIM5 antibodies demonstrated its role in amplifying NF-κB and AP-1 signaling via K63-linked ubiquitin chains, linking capsid recognition to immune activation .
Mitochondrial Quality Control
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Mitophagy Regulation: TRIM5 antibodies identified colocalization with autophagy regulators (ATG13, FIP200) on mitochondrial surfaces, revealing TRIM5’s homeostatic role in Parkin-dependent mitophagy .
Orthpoxvirus Restriction
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Broad Antiviral Activity: TRIM5α-specific antibodies validated its role in restricting vaccinia virus (VACV) replication, while TRIM5γ/δ isoforms showed proviral effects .
Table 2: Recommended Workflows for TRIM5 Antibodies
Product Specs
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze / thaw cycles.
Lead Time
Generally, we can ship the products within 1-3 working days after receiving your orders. Delivery time may vary depending on the purchasing method or location. Please consult your local distributors for specific delivery times.
Synonyms
TRIM5; RNF88; Tripartite motif-containing protein 5; RING finger protein 88; RING-type E3 ubiquitin transferase TRIM5
Target Names
TRIM5
Uniprot No.
Target Background
Function
TRIM5 is a capsid-specific restriction factor that inhibits infection from non-host-adapted retroviruses. It blocks viral replication early in the life cycle, after viral entry but before reverse transcription. Beyond its role as a restriction factor, TRIM5 also functions as a pattern recognition receptor, activating innate immune signaling in response to the retroviral capsid lattice. Upon binding the viral capsid, TRIM5 triggers its E3 ubiquitin ligase activity. In conjunction with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex), it generates 'Lys-63'-linked polyubiquitin chains. These chains act as catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (comprised of TAK1, TAB2, and TAB3). The autophosphorylation activation of the MAP3K7/TAK1 complex leads to the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, ultimately triggering an innate immune response within the infected cell. TRIM5 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). It plays a role in regulating autophagy through activation of the autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. Furthermore, TRIM5 acts as a selective autophagy receptor, recognizing and targeting HIV-1 capsid protein p24 for autophagic destruction.
Gene References Into Functions
- This study demonstrates the feasibility of editing the TRIM5 gene in human cells and identifies the main challenges to be addressed to use this approach to confer protection from HIV-1. PMID: 29373607
- Genetic polymorphism is associated with susceptibility to HIV infections in Brazil. PMID: 27388872
- TRIM5 and TRIM22 single nucleotide polymorphisms are associated with increased odds of significant liver fibrosis and sustained virological response after pegIFNalpha/RBV therapy in human immunodeficiency virus/hepatitis C virus coinfected patients. PMID: 27590274
- TRIM5alpha polymorphisms were associated with proviral loads, indicating a potential role for TRIM5alpha in HTLV-1 replication. PMID: 28420387
- TRIM5alpha potently restricts HIV-1 infection of Langerhans cells but not of subepithelial DC-SIGN+ dendritic cells. PMID: 27919079
- These results are consistent with observations that the turnover of TRIM5alpha proteins is sensitive to autophagy inhibition. However, the data do not support the notion that autophagy inhibition abrogates retroviral restriction by TRIM5 proteins. PMID: 26764007
- This meta-analysis indicates that the TRIM5alpha H43Y polymorphism is associated with a decreased risk of HIV-1 infection in homozygote comparison and recessive model. PMID: 26398573
- These results support the relevance of R332G-R335G and other mutants of TRIM5alphahu as candidate effectors for HIV-1 gene therapy. PMID: 26076730
- Higher-order oligomerization of TRIM5alpha, promoted by interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5alpha and contributes to its antiretroviral function. PMID: 26212332
- Co-immunoprecipitation experiments demonstrate that IE1CORE binds via the coiled-coil domain to PML and also interacts with TRIM5alpha. PMID: 25412268
- Data suggest that due to its lack of stability and inability to accumulate in pronounced cytoplasmic bodies, likely due to its high self-ubiquitination activity, huTRIM5alpha was unable to block HIV-1 infection. PMID: 24662946
- TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34(+) cells in vitro and in vivo. PMID: 24153115
- TRIMs interacts with ULK1 and Beclin 1 and regulates autophagy. PMID: 25127057
- TRIM5 acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5 delivers its cognate cytosolic target, a viral capsid protein, for autophagic degradation. This study establishes that TRIMs can function both as regulators of autophagy and as autophagic cargo receptors, and reveals a basis for selective autophagy in mammalian cells. PMID: 25127057
- TRIM5alpha and TRIM22 have differential transcriptional regulation and distinct anti-HIV roles according to infection phase. PMID: 24478420
- In conclusion, association with microtubules and the translocation activity of dynein motor complexes are required to achieve efficient retrovirus restriction by TRIM5alpha. PMID: 24600008
- Data report that markers in two TRIMs, TRIM5 and TRIM22, and a marker in BST2, are associated statistically with the risk of getting MS. PMID: 24066097
- Our data indicate that although the RhTRIMe7-CypA isoform does not appear to restrict HIV-1, it may act as a negative modulator of TRIM family proteins, presumably by competitive inhibition. PMID: 24613845
- Structural changes exerted on HIV-1 capsid (CA) assembly by TRIM5alpha binding. PMID: 24158810
- Assisted evolution enables HIV-1 to overcome a high TRIM5alpha-imposed genetic barrier to rhesus macaque tropism. PMID: 24086139
- Recruitment to the plasma membrane plays a role in restricting retroviral infection. PMID: 23548691
- This study supports a model in which localized binding of TRIM5 to the retrovirus capsid nucleates rapid polymerization of a TRIM5 lattice on the capsid surface. PMID: 23785198
- HIV-2 capsid sequences expressed high levels of susceptibility to hTRIM5alpha. PMID: 23647667
- Results show how TRIM5alpha affects various retroviral core components and indicate that proteasomes are required for TRIM5alpha-induced core disruption but not for TRIM5alpha-induced restriction. PMID: 23505372
- These data suggest that HIV-1 escapes restriction by TRIM5alpha through the selective disruption of CypA-dependent, TRIM5alpha-mediated inhibition of nuclear import. PMID: 23448277
- Blocking the onset or delaying reverse transcription does not increase HIV-1 sensitivity to TRIM5alpha, indicating that the recognition of the capsids by human TRIM5alpha is completed rapidly, following entry into the cytoplasm. PMID: 23320071
- Amino acid substitution G249D is associated with increased susceptibility to HIV-1 infection. PMID: 23379364
- The recognition of the entire capsid surface is a general strategy for TRIM5alpha to restrict murine leukemia viruses. PMID: 23536686
- Increased sensitivity to TRIM5alpha was observed for some capsid variants, suggesting that minor residues are selected against in human populations. PMID: 23601783
- TRIM5 is a restriction factor that blocks retrovirus infection soon after the virion core enters the cell cytoplasm. Restriction activity is targeted to the virion core via recognition of the capsid protein lattice that encases the viral genomic RNA. [Review] PMID: 22482711
- Findings have defined a novel function for TRIM5 as a pattern recognition receptor in innate immune recognition and provided valuable mechanistic insight into its role as a retroviral restriction factor. PMID: 21866272
- Proteasomal subunits are present in rhTRIM5alpha assemblies containing HIV-1 virions. PMID: 22078707
- Determinants of the higher-order association of the restriction factor TRIM5alpha and other tripartite motif (TRIM) proteins. PMID: 21680743
- TRIM5alpha "cages" the HIV-1 core by forming an hexagonal array on the surface of the viral capsid. PMID: 21994740
- Findings suggest that Gag cytotoxic T lymphocyte mutations may influence HIV-1 replication by modifying both viral infectivity and sensitivity to TRIM5alpha. PMID: 21917976
- This study concludes that interactions involving much, if not all, of the surface of the murine leukemia virus capsid protein are vital for TRIM5alpha binding. PMID: 21483490
- The authors discovered the ability of human and rhesus TRIM5alpha to shuttle into and out of the nucleus. PMID: 21575157
- This review covers the structure and roles of the TRIM5alpha protein, the interaction between Cyp cyclophilin A and TRIM5alpha, as well as gene therapy strategies associated with TRIM5alpha to inhibit HIV-1 infection. [Review] PMID: 21568899
- Knockdown of TRIM5iota increases TRIM5alpha activity in human U373-X4 cells, indicating that physiological levels of expression of truncated TRIM5 isoforms in human cells can reduce the activity of TRIM5. PMID: 21632761
- The SUMO-1-mediated block of murine leukemia virus is mediated by human TRIM5alpha. CA mutations altering the SUMO conjugation sites reduce TRIM5alpha restriction. PMID: 21490953
- The N-terminal region of TRIM5alphaag and TRIM5alphacy are essential for the late restriction activity, while the C-terminal region of TRIM5alphacy negatively regulates the late restriction activity against HIV-1. PMID: 21264255
- The retroviral restriction factor TRIM5 has two additional activities that are linked to restriction: it constitutively promotes innate immune signaling and it acts as a pattern recognition receptor specific for the retrovirus capsid lattice. PMID: 21512573
- Retroviruses have evolved similar mechanisms to escape TRIM5alpha restriction via the interference of structurally homologous determinants in the viral capsid. PMID: 21169362
- The authors concluded that H43Y might account for the HIV-1 resistance due to TRIM5alpha gene in Chinese intravenous drug users. PMID: 21107267
- Innate immunity mediated by the envelope of murine leukemia virus in human cells is TRIM5alpha independent. PMID: 20929586
- TRIM5alpha proteins have evolved to restrict a range of different retroviruses by assembling a deformable hexagonal scaffold that positions the capsid-binding domains to match the symmetry and spacing of the capsid surface lattice. PMID: 21187419
- Both common and rare variants of TRIM5alpha are associated with the susceptibility to HIV-1 infection in Japanese and Indian subjects. PMID: 19710594
- The ability of human Trim5alpha to regulate TAB2 levels, to activate NF-kappaB, and to recognize retroviral capsids are genetically separable. PMID: 21035162
- These findings suggest that human TRIM5alpha is an intrinsic immunity factor against HIV-1 infection. PMID: 20493962
- Cytoplasmic body component TRIM5{alpha} requires lipid-enriched microdomains for efficient HIV-1 restriction. PMID: 20810659
Database Links
Protein Families
TRIM/RBCC family
Subcellular Location
Cytoplasm. Nucleus.
Customer Reviews
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B.A
By Anonymous
★★★★★
Applications : Western Blot
Sample type: Muscle Myo-lineage cells
Review: In order to verify the reliability of proteomics data, 7 DEPs were randomly selected for Western blot analysis. As shownin FigureS1, there lativea bundance sof selected proteins between Myo-L and Myo-Y determined by Western blot were highly consistent with the data of TMT analysis.
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