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  4. TRIM5 Antibody

TRIM5 Antibody

  • 货号：
    CSB-PA024488GA01HU
  • 规格：
    ￥3,900
  • 其他：

产品详情

  • Uniprot No.：
    Q9C035
  • 基因名：
    TRIM5
  • 别名：
    TRIM5; RNF88; Tripartite motif-containing protein 5; RING finger protein 88; RING-type E3 ubiquitin transferase TRIM5
  • 宿主：
    Rabbit
  • 反应种属：
    Human
  • 免疫原：
    Human TRIM5
  • 免疫原种属：
    Homo sapiens (Human)
  • 抗体亚型：
    IgG
  • 纯化方式：
    Antigen Affinity Purified
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 保存缓冲液：
    PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA,IHC
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

产品评价

靶点详情

  • 功能：
    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). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. 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.
  • 基因功能参考文献：
    1. study demonstrates the feasibility of editing the TRIM5 gene in human cells and identifies the main challenges to be addressed in order to use this approach to confer protection from HIV-1 PMID: 29373607
    2. genetic polymorphism is associated with susceptibility to HIV infections in Brazil PMID: 27388872
    3. TRIM5 and TRIM22 single nucleotide polymorphisms are associated to 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
    4. TRIM5alpha polymorphisms were associated with proviral loads, indicating that TRIM5alpha could be implicated in HTLV-1 replication. PMID: 28420387
    5. TRIM5alpha potently restricts HIV-1 infection of Langerhans cells but not of subepithelial DC-SIGN+ dendritic cells PMID: 27919079
    6. Collectively, these results are consistent with observations that the turnover of TRIM5alpha proteins is sensitive to autophagy inhibition; however, the data presented here do not support observations that the inhibition of autophagy abrogates retroviral restriction by TRIM5 proteins. PMID: 26764007
    7. This meta-analysis indicates that TRIM5alpha H43Y polymorphism is associated with a decreased risk of HIV-1 infection in the homozygote comparison and recessive model. PMID: 26398573
    8. These results support the relevance of R332G-R335G and other mutants of TRIM5alphahu as candidate effectors for HIV-1 gene therapy. PMID: 26076730
    9. higher-order oligomerization of TRIM5alpha, which is promoted by the interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5alpha and contributes to its antiretroviral function. PMID: 26212332
    10. co-immunoprecipitation experiments demonstrate that IE1CORE binds via the coiled-coil domain to PML and also interacts with TRIM5alpha PMID: 25412268
    11. 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
    12. TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34(+) cells in vitro and in vivo. PMID: 24153115
    13. TRIMs interacts with ULK1 and Beclin 1 and regulates autophagy. PMID: 25127057
    14. TRIM5 acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5 delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation. Thus, our 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
    15. TRIM5alpha and TRIM22 have differential transcriptional regulation and distinct anti-HIV roles according to infection phase. PMID: 24478420
    16. In conclusion, association with microtubules and the translocation activity of dynein motor complexes are required to achieve efficient retrovirus restriction by TRIM5alpha. PMID: 24600008
    17. Data report that markers in two TRIMs, TRIM5 and TRIM22 and a marker in BST2, associated statistically with the risk of getting MS. PMID: 24066097
    18. 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
    19. structural changes exerted on HIV-1 capsid (CA) assembly by TRIM5alpha binding PMID: 24158810
    20. Assisted evolution enables HIV-1 to overcome a high TRIM5alpha-imposed genetic barrier to rhesus macaque tropism. PMID: 24086139
    21. recruitment to the plasma membrane plays role in restriction of retroviral infection PMID: 23548691
    22. These 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
    23. HIV-2 capsid sequences expressed high levels of susceptibility to hTRIM5alpha. PMID: 23647667
    24. 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
    25. 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
    26. 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
    27. amino acid substitution G249D associated with increased susceptibility to HIV-1 infection PMID: 23379364
    28. The recognition of the entire capsid surface is a general strategy for TRIM5alpha to restrict murine leukemia viruses. PMID: 23536686
    29. Increased sensitivity to TRIM5alpha was observed for some capsid variants, suggesting that minor residues are selected against in human populations. PMID: 23601783
    30. 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
    31. 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
    32. Proteasomal subunits are present in rhTRIM5alpha assemblies containing HIV-1 virions. PMID: 22078707
    33. Determinants of the higher order association of the restriction factor TRIM5alpha and other tripartite motif (TRIM) proteins. PMID: 21680743
    34. TRIM5alpha "cages" the HIV-1 core by forming an hexagonal array on the surface of the viral capsid. PMID: 21994740
    35. findings suggest that Gag cytotoxic T lymphocyte mutations may influence HIV-1 replication by modifying both viral infectivity and sensitivity to TRIM5alpha PMID: 21917976
    36. 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
    37. The s discovered the ability of human and rhesus TRIM5alpha to shuttle into and out of the nucleus. PMID: 21575157
    38. review of the structure and roles of 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
    39. 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
    40. 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
    41. 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
    42. the retroviral restriction factor TRIM5 has two additional activities that are linked to restriction: it constitutively promotes innate immune signalling and it acts as a pattern recognition receptor specific for the retrovirus capsid lattice PMID: 21512573
    43. retroviruses have evolved similar mechanisms to escape TRIM5alpha restriction via the interference of structurally homologous determinants in the viral capsid. PMID: 21169362
    44. The s concluded that H43Y might account for the HIV-1 resistance due to TRIM5alpha gene in Chinese intravenous drug users. PMID: 21107267
    45. Innate immunity mediated by envelope of murine leukemia virus in human cells is TRIM5alpha independent. PMID: 20929586
    46. 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
    47. Both common and rare variants of TRIM5alpha are associated with the susceptibility to HIV-1 infection in Japanese and Indian subjects. PMID: 19710594
    48. The ability of human Trim5alpha to regulate TAB2 levels, to activate NF-kappaB, and to recognize retroviral capsids are genetically separable. PMID: 21035162
    49. These findings suggest that human TRIM5alpha is an intrinsic immunity factor against HIV-1 infection. PMID: 20493962
    50. Cytoplasmic body component TRIM5{alpha} requires lipid-enriched microdomains for efficient HIV-1 restriction. PMID: 20810659

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  • 亚细胞定位：
    Cytoplasm. Nucleus.
  • 蛋白家族：
    TRIM/RBCC family
  • 数据库链接：

    HGNC: 16276

    OMIM: 608487

    KEGG: hsa:85363

    STRING: 9606.ENSP00000369373

    UniGene: Hs.125300