Recombinant Human TRIM5 Protein (N-6His)

Name: Recombinant Human TRIM5 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1561NP
Availability: InStock

BL-1561NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Tripartite Motif-containing Protein 5 is produced by our E.coli expression system and the target gene encoding Met1-Gln248 is expressed with a 6His tag at the N-terminus.
Accession	Q9C035
Synonym	Tripartite motif-containing protein 5;RING finger protein 88;TRIM5;RNF88
Gene Background	Tripartite motif-containing Motif 5 is a protein that in humans is encoded by the TRIM5 gene.It is a 493 amino acids protein that belongs to the TRIM/RBCC family.It contains 1 B box-type zinc finger, 1 B30.2/SPRY domain and 1 RING-type zinc finger. TRIM5 present in the cytoplasm recognizes motifs within the capsid proteins and interferes with the uncoating process, therefore preventing successful reverse transcription and transport to the nucleus of the viral genome. The exact mechanism of action has not been shown conclusively, but capsid protein from restricted viruses is removed by proteasome-dependent degradation
Molecular Mass	30.8 KDa
Apmol Mass	30-36 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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	HGNC: 16276 OMIM: 608487 KEGG: hsa:85363 STRING: 9606.ENSP00000369373 UniGene: PMID: 29373607 genetic polymorphism is associated with susceptibility to HIV infections in Brazil PMID: 27388872 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 TRIM5alpha polymorphisms were associated with proviral loads, indicating that TRIM5alpha could be implicated 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 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 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 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, 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 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 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 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, 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 role in restriction of retroviral infection PMID: 23548691 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 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 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 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 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 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 signalling 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 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

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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.

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Recombinant Human TRIM5 Protein (N-6His)

Recombinant Human TRIM5 Protein (N-6His)

Product Overview

Target Details

FAQs