Recombinant Human TRIM5 delta Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9205P

Recombinant Human TRIM5 delta Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9205P
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Product Overview

Host Species Human
Accession Q9C035
Synonym EG667823 Gm8833 RING finger protein 88 RNF88 TRIM5 TRIM5_HUMAN Tripartite motif containing 5 transcript variant iota Tripartite motif containing 5 transcript variant kappa Tripartite motif containing protein 5 Tripartite motif protein TRIM5 Tripartite motif-containing protein 5
Description Recombinant Human TRIM5 delta Protein (His tag) was expressed in HEK293. It is a Protein fragment
Source HEK293
AA Sequence MGSSHHHHHHSSGLVPRGSHMASGILVNVKEEVTCPICLELLTQPLSLDC GHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKL REVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFL TEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTN VLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRE LISDLEHRLQGSVMELLQ
Molecular Weight 31 kDa including tags
Purity Greater than 95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on Dry Ice. Store at -80°C.

Target Details

Target 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). 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.
Subcellular Location Cytoplasm. Nucleus.
Protein Families TRIM/RBCC family
Database References

Gene Functions References

  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 authors 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 authors 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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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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