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AB196078

Recombinant Human TRIM5 delta protein (His tag)

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Recombinant Human TRIM5 delta protein (His tag) is a Human Fragment protein, in the 1 to 248 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

RNF88, TRIM5, Tripartite motif-containing protein 5, RING finger protein 88, RING-type E3 ubiquitin transferase TRIM5

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag N-Terminus

Applications

SDS-PAGE, HPLC

applications

Biologically active

No

Accession

Q9C035

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 99% Phosphate Buffer, 0.87% Sodium chloride

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQ","proteinLength":"Fragment","predictedMolecularWeight":"30.85 kDa","actualMolecularWeight":null,"aminoAcidEnd":248,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q9C035","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

TRIM5 delta an alternate isoform of the TRIM5 protein functions as a part of the tripartite motif family. TRIM5 delta includes a RING domain B-box type 2 and a coiled-coil region with a single mass of approximately 57 kDa. It is expressed in various tissues including lymphoid organs and cells involved in the immune response. The isoform structurally differs from other TRIM5 variants notably due to the absence of the C-terminal PRYSPRY domain which affects its binding capabilities.
Biological function summary

TRIM5 delta participates in the innate immune defense mechanism against retroviral infections. Although the delta isoform lacks the PRYSPRY domain it still contributes to the restriction of retroviruses through an alternative mechanism involving protein oligomerization. TRIM5 delta does not form a part of large macromolecular complexes like full-length TRIM5 proteins do. Its unique structure enables distinct interactions which may impact its antiviral function independently or synergistically with other forms of TRIM5.

Pathways

Several innate immunity and antiviral defense pathways include functions of TRIM5 delta. An important pathway involves the disruption of the viral capsid after uncoating. TRIM5 delta associates with proteins such as TRIMCyp with the shared goal of impeding viral replication. The specific signaling cascade remains under exploration though it is evident TRIM5 delta modulates critical steps of the host's antiviral response contrasting other isoforms.

TRIM5 delta has associations with HIV infection resistance and autoimmune conditions. Alterations in the structure and effectiveness of TRIM5 delta can impact susceptibility to HIV offering potential insight into resistance mechanisms that other TRIM5 isoforms might not provide. Connections to autoimmune activity emerge through interaction with proteins like TRIM21 which also participate in immune regulation and response suggesting a broader role in immune system homeostasis. Understanding these relationships aids in grasping TRIM5 delta’s potential impact on disease treatment and prevention strategies.
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Specifications

Form

Liquid

Additional notes

The purity of ab196078 is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.

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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

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Product protocols

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Target data

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).
See full target information TRIM5
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