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TRIM21 / RO52 Antibody (C-Terminus)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | P19474 |
| Reactivity | Human, Monkey |
| Host | Goat |
| Clonality | Polyclonal |
| Calculated MW | 54kDa |
| Dilution | ELISA (1:32000), IHC-P (5 µg/ml), |
| Gene ID | 6737 |
|---|---|
| Other Names | E3 ubiquitin-protein ligase TRIM21, 6.3.2.-, 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, RING finger protein 81, Ro(SS-A), Sjoegren syndrome type A antigen, SS-A, Tripartite motif-containing protein 21, TRIM21, RNF81, RO52, SSA1 |
| Target/Specificity | Human TRIM21. |
| Reconstitution & Storage | Store at -20°C. Minimize freezing and thawing. |
| Precautions | TRIM21 / RO52 Antibody (C-Terminus) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | TRIM21 (HGNC:11312) |
|---|---|
| Synonyms | RNF81, RO52, SSA1 |
| Function | E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2 (PubMed:26347139, PubMed:16297862, PubMed:16316627, PubMed:16472766, PubMed:16880511, PubMed:18022694, PubMed:18361920, PubMed:18641315, PubMed:18845142, PubMed:19675099). 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). |
| Cellular Location | Cytoplasm. Cytoplasmic vesicle, autophagosome. Nucleus. Cytoplasm, P-body. Cytoplasm, Stress granule. Note=Enters the nucleus upon exposure to nitric oxide (PubMed:18361920). Localizes to small dot- or rod-like structures in the cytoplasm, called processing bodies (P-bodies) that are located underneath the plasma membrane and also diffusely in the cytoplasm (PubMed:18361920). They are located along the microtubules and are highly motile in cells (PubMed:18361920). Colocalizes with DCP2 in P-bodies (PubMed:18361920). Localizes to stress granules in response to oxidative stress (PubMed:36692217). |
| Tissue Location | Isoform 1 and isoform 2 are expressed in fetal and adult heart and fetal lung |
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Provided below are standard protocols that you may find useful for product applications.
Background
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. 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. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. 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. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin- mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.
References
Itoh K.,et al.J. Clin. Invest. 87:177-186(1991).
Chan E.K.,et al.J. Clin. Invest. 87:68-76(1991).
Tsugu H.,et al.Genomics 24:541-548(1994).
Keech C.L.,et al.Clin. Exp. Immunol. 104:255-263(1996).
Bepler G.,et al.Genomics 55:164-175(1999).
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