Recombinant Human TRIM21/SS-A protein (GST tag N-Terminus)
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Recombinant Human TRIM21/SS-A protein (GST tag N-Terminus) is a Human Fragment protein, in the 68 to 175 aa range, expressed in Wheat germ, with >80%, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
RNF81, RO52, SSA1, TRIM21, E3 ubiquitin-protein ligase TRIM21, 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, RING finger protein 81, Ro(SS-A), Sjoegren syndrome type A antigen, Tripartite motif-containing protein 21, SS-A
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human TRIM21/SS-A protein (GST tag N-Terminus) (AB114611)
ab114611 analysed on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
TRIM21 contributes significantly to the regulation of immune responses and participates in innate and adaptive immunity. It forms part of a complex with other proteins to facilitate the degradation of viral particles through the ubiquitin-proteasome system a process known as antibody-dependent intracellular neutralization. As an important player in the immune defense TRIM21 oversees the timely removal of pathogens and prevents potential overactivation of immune responses that might harm the host.
Pathways
TRIM21 operates within the interferon signaling and NF-κB pathways two important areas of immune response modulation. TRIM21 interacts with molecules like transcription factors that influence the expression of interferon-responsive genes which are critical for pathogen defense. Its role in these pathways highlights its interactions with various immune-regulatory proteins helping to maintain immune system balance and effectiveness during infections.
Specifications
Form
Liquid
Additional notes
Glutathione Sepharose
General info
Function
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2 (PubMed : 16297862, PubMed : 16316627, PubMed : 16472766, PubMed : 16880511, PubMed : 18022694, PubMed : 18361920, PubMed : 18641315, PubMed : 18845142, PubMed : 19675099, PubMed : 26347139). Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination (PubMed : 16880511, PubMed : 19675099). Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes (PubMed : 16880511). A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome (PubMed : 16880511). Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling (PubMed : 19675099). Negatively regulates IFN-beta production post-pathogen recognition by catalyzing polyubiquitin-mediated degradation of IRF3 (PubMed : 18641315). Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway (PubMed : 18022694). Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages (By similarity). Plays a role in the regulation of the cell cycle progression (PubMed : 16880511). Enhances the decapping activity of DCP2 (PubMed : 18361920). Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules (PubMed : 1985094, PubMed : 8666824). At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified (PubMed : 8666824). The common feature of these proteins is their ability to bind HY RNAs.2 (PubMed : 8666824). Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed : 26347139). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed : 26347139). Regulates also autophagy through FIP200/RB1CC1 ubiquitination and subsequent decreased protein stability (PubMed : 36359729). Represses the innate antiviral response by facilitating the formation of the NMI-IFI35 complex through 'Lys-63'-linked ubiquitination of NMI (PubMed : 26342464). During viral infection, promotes cell pyroptosis by mediating 'Lys-6'-linked ubiquitination of ISG12a/IFI27, facilitating its translocation into the mitochondria and subsequent CASP3 activation (PubMed : 36426955). When up-regulated through the IFN/JAK/STAT signaling pathway, promotes 'Lys-27'-linked ubiquitination of MAVS, leading to the recruitment of TBK1 and up-regulation of innate immunity (PubMed : 29743353). Mediates 'Lys-63'-linked polyubiquitination of G3BP1 in response to heat shock, leading to stress granule disassembly (PubMed : 36692217).
Sequence similarities
Belongs to the TRIM/RBCC family.
Post-translational modifications
Autoubiquitinated; does not lead to its proteasomal degradation. Deubiquitinated by USP4; leading to its stabilization.
Subcellular localisation
Nucleus
Target data
Product promise
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