Recombinant Human TRIM5 alpha protein (Tagged)
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Recombinant Human TRIM5 alpha protein (Tagged) is a Human Full Length protein, in the 1 to 493 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
RNF88, TRIM5, Tripartite motif-containing protein 5, RING finger protein 88, RING-type E3 ubiquitin transferase TRIM5
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human TRIM5 alpha protein (Tagged) (AB239570)
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel analysis of ab239570.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
TRIM5 alpha functions as an innate immune factor that interferes with early stages of retroviral infections in host cells. It does not function alone; it is part of a complex including other TRIM proteins that work together to recognize and block the reverse transcription of viral RNA into DNA. This action prevents viral replication at very early stages providing antiviral defenses even before adaptive immunity kicks in.
Pathways
TRIM5 alpha plays a significant role in the innate immune pathway specifically influencing the recognition and response to retroviral infections. It interacts with proteins like cyclophilin A to enhance its ability to restrict retroviruses like HIV-1. TRIM5 alpha activity also connects with the ubiquitin-proteasome system facilitating the degradation of viral components that enter host cells reducing the potential for infection.
Specifications
Form
Liquid
General info
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) (PubMed : 17156811). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed : 25127057). 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 (PubMed : 25127057).
Sequence similarities
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.
Subcellular localisation
Nucleus
Target data
Product promise
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