E3 ubiquitin-protein ligase TRIM21 Recombinant Protein | RO52 recombinant protein

Recombinant Homo sapiens E3 ubiquitin-protein ligase TRIM21

Cat. Num. AAA9422534

• Gene Names: TRIM21; SSA; RO52; SSA1; RNF81; Ro/SSA
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase TRIM21; Recombinant Homo sapiens E3 ubiquitin-protein ligase TRIM21; 52 kDa Ro protein; 52 kDa ribonucleoprotein auto; antigen Ro/SS-ARING finger protein 81Ro (SS-A); Sjoegren syndrome type A antigen; SS-A; Tripartite motif-containing protein 21; RO52 recombinant protein

• Host: Yeast
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Tris-based buffer 50% glycerol
• Sequence Positions: 1-475aa, Full Length
• Sequence: MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY

• Tag Info: N-Terminal 6xHis-tagged
• Preparation and Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C, -80°C. The shelf life of lyophilized form is 12 months at -20°C, -80°C.; ; Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Related Product Information for RO52 recombinant protein

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

NCBI and Uniprot Product Information

• NCBI GI #: 15208660
• NCBI GeneID: 6737
• NCBI Accession #: NP_003132.2
• NCBI GenBank Nucleotide #: NM_003141.3
• UniProt Accession #: P19474; Q5XPV5; Q96RF8
• Molecular Weight: 56.2 kDa
• NCBI Official Full Name: E3 ubiquitin-protein ligase TRIM21
• NCBI Official Synonym Full Names: tripartite motif containing 21
• NCBI Official Symbol: TRIM21
• NCBI Official Synonym Symbols: SSA; RO52; SSA1; RNF81; Ro/SSA
• NCBI Protein Information: E3 ubiquitin-protein ligase TRIM21
• UniProt Protein Name: E3 ubiquitin-protein ligase TRIM21
• Protein Family: E3 ubiquitin-protein ligase
• UniProt Gene Name: TRIM21
• UniProt Synonym Gene Names: RNF81; RO52; SSA1; SS-A

NCBI Description

This gene encodes 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 encoded protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. RoSSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Alternatively spliced transcript variants for this gene have been described but the full-length nature of only one has been determined. [provided by RefSeq, Jul 2008]

Uniprot Description

TRIM21: 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. Belongs to the TRIM/RBCC family. 2 isoforms of the human protein are produced by alternative splicing.

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

Chromosomal Location of Human Ortholog: 11p15.4

Cellular Component: cytoplasm; cytosol; nucleoplasm; nucleus; ribonucleoprotein complex; SCF ubiquitin ligase complex

Molecular Function: identical protein binding; protein binding; ubiquitin-protein ligase activity

Biological Process: inhibition of NF-kappaB transcription factor; innate immune response; negative regulation of viral transcription; positive regulation of autophagy; positive regulation of cell cycle; positive regulation of transcription factor activity; protein autoubiquitination; protein destabilization; protein monoubiquitination; protein polyubiquitination; protein ubiquitination; regulation of interferon type I production