Rabbit anti-Human Trim5 alpha Polyclonal Antibody | anti-TRIM5 antibody

Trim5 alpha Antibody

Cat. Num. AAA9630854

• Gene Names: TRIM5; RNF88; TRIM5alpha
• Reactivity: Human
• Applications: ELISA
• Purity: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Synonyms: Trim5 alpha; Polyclonal Antibody; Trim5 alpha Antibody; RING finger protein 88; RNF88; TRIM5; TRIM5_HUMAN; tripartite motif protein TRIM5; Tripartite motif-containing protein 5; anti-TRIM5 antibody

• Host: Rabbit
• Reactivity: Human
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Trim5 alpha Antibody detects endogenous levels of Trim5 alpha.
• Purity/Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink Coupling Resin (Thermo Fisher Scientific).
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-TRIM5 antibody: ELISA (EIA)(peptide)
• Application Notes: ELISA(peptide): 1:20000-1:40000
• Immunogen: A synthesized peptide derived from human Trim5 alpha.
• Conjugation: Unconjugated
• Similarity: The B box-type zinc finger domain and the coiled-coil domain contribute to the higher and low order multimerization respectively which is essential for restriction activity (PubMed:22482711). The coiled coil domain is important for higher order multimerization by promoting the initial dimerization (By similarity). The B30. 2/SPRY domain acts as a capsid recognition domain. Polymorphisms in this domain explain the observed species-specific differences among orthologs (PubMed:22482711). The RING-type zinc finger domain confers E3 ubiquitin ligase activity and is essential for retrovirus restriction activity, autoubiquitination and higher-order multimerization. Belongs to the TRIM/RBCC family.
• Post Translational Modifications: 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.
• Subunit Structure: Can form homodimers and homotrimers. In addition to lower-order dimerization, also exhibits a higher-order multimerization and both low- and high-order multimerizations are essential for its restriction activity. Isoform Delta interacts with BTBD1 and BTBD2. Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70 (By similarity). Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with PSMC2, MAP3K7/TAK1, TAB2 and TAB3. Interacts with SQSTM1. Interacts with TRIM6 and TRIM34. Interacts with ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, MAP1LC3C and BECN1.
• 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.
• Note: 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).
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Product Categories/Family for anti-TRIM5 antibody

Cytoplasm; Nucleus; Primary

NCBI and Uniprot Product Information

• NCBI GI #: 15011944
• NCBI GeneID: 85363
• NCBI Accession #: NP_149083
• NCBI GenBank Nucleotide #: NM_033092.1
• UniProt Accession #: Q9C035; Q2MLV4; Q2MLV8; Q2MLV9; Q2MLW1; Q2MLW3; Q2MLW4; A6NGQ1; A8WFA8; D3DQS8; D3DQS9; G3GJY1
• Molecular Weight: 29,677 Da
• NCBI Official Full Name: tripartite motif protein TRIM5 isoform gamma
• NCBI Official Synonym Full Names: tripartite motif containing 5
• NCBI Official Symbol: TRIM5
• NCBI Official Synonym Symbols: RNF88; TRIM5alpha
• NCBI Protein Information: tripartite motif-containing protein 5; ring finger protein 88; tripartite motif protein TRIM5; tripartite motif containing 5 transcript variant iota; tripartite motif containing 5 transcript variant kappa
• UniProt Protein Name: Tripartite motif-containing protein 5
• Protein Family: Tripartite motif-containing protein
• UniProt Gene Name: TRIM5
• UniProt Synonym Gene Names: RNF88
• UniProt Entry Name: TRIM5_HUMAN

NCBI Description

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]

Uniprot Description

TRIM5: Isoform Alpha is a retrovirus restriction factor, which mediates species-specific, early block to retrovirus infection. Targets retroviral capsid soon after entry into the cell, and prevents reverse transcription of the virus RNA genome. Isoform Alpha trimers may make multiple contacts with the hexameric lattice of CA proteins which constitute the surface of retrovirion core, and somehow inactivate the virus. Restricts efficiently infection by N-MLV, but not HIV-1. May have E3 ubiquitin-protein ligase activity. Belongs to the TRIM/RBCC family. 6 isoforms of the human protein are produced by alternative splicing.

Protein type: Ubiquitin ligase; Ligase; EC 6.3.2.19; EC 6.3.2.-; Ubiquitin conjugating system

Chromosomal Location of Human Ortholog: 11p15

Cellular Component: cytoplasm; cytosol

Molecular Function: identical protein binding; protein binding; protein homodimerization activity; zinc ion binding; ubiquitin-protein ligase activity; pattern recognition receptor activity; ligase activity

Biological Process: positive regulation of I-kappaB kinase/NF-kappaB cascade; viral reproduction; positive regulation of MAPKKK cascade; negative regulation of virion penetration into host cell; cytokine and chemokine mediated signaling pathway; innate immune response; positive regulation of transcription factor activity; pattern recognition receptor signaling pathway; defense response to virus; activation of innate immune response; regulation of lipopolysaccharide-mediated signaling pathway; activation of NF-kappaB transcription factor