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

Recombinant mouse E3 ubiquitin-protein ligase TRIM21

Cat. Num. AAA9421210

• Gene Names: Trim21; Ro52; Ssa1
• Reactivity: Mouse
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: E3 ubiquitin-protein ligase TRIM21; Recombinant mouse E3 ubiquitin-protein ligase TRIM21; 52 kDa Ro protein; 52 kDa ribonucleo; protein autoantigen Ro/SS-ARo (SS-A); Sjoegren syndrome type A antigen; SS-A; Tripartite motif-containing protein 21; RO52 recombinant protein

• Host: E Coli
• Reactivity: Mouse
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: Tris-based buffer 50% glycerol
• Sequence Positions: Full Length, 1-470aa

• Immunogen: Expression Region:1-470aaSequence; Info:Full Length
• Target Sequence: MSPSTTSKMSLEKMWEEVTCSICLDPMVEPMSIECGHCFCKECIFEVGKNGGSSCPECRQQ; FLLRNLRPNRHIANMVENLKQIAQNTKKSTQETHCMKHGEKLHLFCEEDGQALCWVCAQSGKHRDHTRVPI; EEAAKVYQEKIHVVLEKLRKGKELAEKMEMDLTMQRTDWKRNIDTQKSRIHAEFALQNSLLAQEEQRQLQR; LEKDQREYLRLLGKKEAELAEKNQALQELISELERRIRGSELELLQEVRIILERSGSWNLDTLDIDAPDLT; STCPVPGRKKMLRTCWVHITLDRNTANSWLIISKDRRQVRMGDTHQNVSDNKERFSNYPMVLGAQRFSSGK; MYWEVDVTQKEAWDLGVCRDSVQRKGQFSLSPENGFWTIWLWQDSYEAGTSPQTTLHIQVPPCQIGIFVDY; EAGVVSFYNITDHGSLIYTFSECVFAGPLRPFFNVGFNYSGGNAAPLKLCPLKM
• Tag Info: N-terminal 6xHis-SUMO-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 #: 3024571
• NCBI GeneID: 20821
• UniProt Accession #: Q62191
• Molecular Weight: 70.2 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: Ro52; Ssa1
• 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: Ro52; Ssa1; SS-A

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: 7|7 E3

Cellular Component: cytoplasm; nucleoplasm; nucleus; 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; positive regulation of virion penetration into host cell; protein autoubiquitination; protein destabilization; protein monoubiquitination; protein polyubiquitination; protein ubiquitination