Recombinant Human E3 Ubiquitin-Protein Ligase Trim21 (TRIM21) Protein (His)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Trim21 (TRIM21) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03683P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) TRIM21.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Trim21 (TRIM21) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P19474
Target Symbol	TRIM21
Synonyms	52 kDa ribonucleoprotein autoantigen Ro/SS-A; 52 kDa Ro protein; 52kD Ro/SSA autoantigen; Autoantigen Ro/SSA, 52-KD; E3 ubiquitin-protein ligase TRIM21; RING finger protein 81; RNF81; Ro 52; Ro(SS-A); Ro52; RO52_HUMAN; Sicca syndrome antigen A; Sjoegren syndrome type A antigen; Sjogren syndrome antigen A1; Sjogren syndrome type A antigen; SS-A; SSA; SSA1: Sjogren syndrome antigen A1 (52kDa ribonucleoprotein autoantigen SS-A/Ro); TRIM21; Tripartite motif protein TRIM21; Tripartite motif-containing 21; Tripartite motif-containing protein 21
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECISQVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEAREGTQGERCAVHGERLHLFCEKDGKALCWVCAQSRKHRDHAMVPLEEAAQEYQEKLQVALGELRRKQELAEKLEVEIAIKRADWKKTVETQKSRIHAEFVQQKNFLVEEEQRQLQELEKDEREQLRILGEKEAKLAQQSQALQELISELDRRCHSSALELLQEVIIVLERSESWNLKDLDITSPELRSVCHVPGLKKMLRTCAVHITLDPDTANPWLILSEDRRQVRLGDTQQSIPGNEERFDSYPMVLGAQHFHSGKHYWEVDVTGKEAWDLGVCRDSVRRKGHFLLSSKSGFWTIWLWNKQKYEAGTYPQTPLHLQVPPCQVGIFLDYEAGMVSFYNITDHGSLIYSFSECAFTGPLRPFFSPGFNDGGKNTAPLTLCPLNIGSQGSTDY
Expression Range	1-475aa
Protein Length	Full Length
Mol. Weight	58.2 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 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.

Target Details

Target Function	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. Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. 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. Acts as an autophagy receptor for the degradation of IRF3, hence attenuating type I interferon (IFN)-dependent immune responses. Represses the innate antiviral response by facilitating the formation of the NMI-IFI35 complex through 'Lys-63'-linked ubiquitination of NMI.
Subcellular Location	Cytoplasm. Cytoplasmic vesicle, autophagosome. Nucleus. Cytoplasm, P-body. Note=Enters the nucleus upon exposure to nitric oxide. 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. They are located along the microtubules and are highly motile in cells. Colocalizes with DCP2 in P-bodies.
Protein Families	TRIM/RBCC family
Database References	HGNC: 11312 OMIM: 109092 KEGG: hsa:6737 STRING: 9606.ENSP00000254436 UniGene: PMID: 29511085 The expression of TRIM21 mRNA and protein was significantly higher in Systemic lupus erythematosus PBMCs as compared to healthy controls. There was a correlation between TRIM21 mRNA expression and Systemic lupus erythematosus activities. PMID: 29385873 Low TRIM21 expression is associated with RNA virus infections. PMID: 29743353 TRIM21 positively regulated osteosarcoma cell proliferation. Overexpression of TRIM21 enhanced osteosarcoma cell tolerance toward various stresses. YWHAZ protein was identified as a novel interacting partner of TRIM21 and its expression levels were negatively regulated by TRIM21. PMID: 29673441 expression increased in lesional psoriatic skin PMID: 27943421 when misfolded tau assemblies enter the cell, they can be detected and neutralized via a danger response mediated by tau-associated antibodies and the cytosolic Fc receptor tripartite motif protein 21 (TRIM21) PMID: 28049840 Taken together, the current study provides evidence of new function of Ro60/SSA in the development of cancer. It facilitates pancreatic cancer proliferation, migration and invasion. Therefore, it may represent a novel molecular target for the management of pancreatic cancer. PMID: 29274781 We suggest that TRIM21 may be one of the factors associated with the "switching on" the proinflammatory programme in CD16(+) monocytes or monocyte-derived macrophages. PMID: 27773663 Authors demonstrate that TRIM21 expression predicts survival in pancreatic cancer patients. This work highlights a novel mechanism of Par-4 regulation, and identifies a novel prognostic marker and potential therapeutic target for pancreatic cancer. PMID: 27830973 TRIM21 role in TRAIL-induced apoptosis PMID: 27219672 Our data suggest that patients with IIM, mainly DM, are characterized by a deficient expression of Ro52/TRIM21 in different PBMC subsets (CD4(+) lymphocytes and monocytes), along with lower K48-mediated ubiquitination, which is associated with a proinflammatory cytokine response. PMID: 27936488 Significant relationships were found between clinical and laboratory manifestations of autoimmune and rheumatic diseases with different patterns of antibodies to anti-Ro52, anti-Ro60 and anti-La . PMID: 26725021 downregulation of miR-1207-5p and miR-4695-3p expression may lead to increased TRIM21 levels in the minor salivary glands, which contributes to the development of Sjogren's syndrome PMID: 26888739 The interaction of TRIM21 and LFG was analyzed by co-immunoprecipitation. To examine changes in regulatory processes, western blot analyses, real-time PCR, activity of apoptotic process and flow cytometric analyses were carried out. PMID: 26398169 TRIM21 plays an essential role in p62-regulated redox homeostasis and may be a viable target for treating pathological conditions resulting from oxidative damage. PMID: 26942676 TRIM21-induced exposure of the viral genome promotes sensing of DNA and RNA viruses by cGAS and RIG-I PMID: 26506431 we prove that TRIM21 is a potential tumor suppressor in hepatocellular carcinoma and its low expression indicates poor prognosis PMID: 26055142 Trim21 regulates Nmi-IFI35 complex-mediated inhibition of innate antiviral response PMID: 26342464 TRIM20 and TRIM21 mediate precision autophagy, controlling the hub signaling machineries and key factors, inflammasome and type I interferon, directing cardinal innate immunity response systems in humans. PMID: 26347139 This study elucidates a complex mechanism of step-wise ubiquitination and deubiquitination activities that allows contemporaneous innate immune signaling and neutralization by TRIM21. PMID: 26150489 Anti-Ro52/TRIM21 antibodies are independently associated with the presence of interstitial lung disease and poor survival in systemic sclerosis. PMID: 26315678 Endoplasmic reticulum stress causes autophagy and apoptosis leading to cellular redistribution of the SS-A and SS-B autoantigens in salivary gland epithelial cells of Sjogren's syndrome patients. PMID: 25845745 These data extend the protective role of TRIM21 from viruses to bacteria and thereby strengthening the general role of antibody-dependent intracellular neutralisation in cellular immunity. PMID: 24920099 Upregulation of SSA1 is associated with alcoholic and nonalcoholic steatohepatitis. PMID: 25526666 TRIpartite motif 21 (TRIM21) differentially regulates the stability of interferon regulatory factor 5 (IRF5) isoforms. PMID: 25084355 Report association of Anti-Ro/SSA-p200 antibodies with congenital heart block. PMID: 25327946 Although protein expression levels were not affected significantly, the late up-regulation of Ro52/TRIM21 mRNA was accompanied by protein redistribution PMID: 25098814 the up-regulation of Ro52 in ductal epithelium might be a triggering factor for disease progression in Sjogren's syndrome. PMID: 24673429 Cytoplasmic sequestration of GMPS requires ubiquitylation by TRIM21. PMID: 24462112 epitope peptide of the TRIM21 (TRIM: tripartite motif) autoantigen that is recognized by a polyclonal antibody was determined as assembling an "L-E-Q-L" motif on an alpha-helix PMID: 24094071 Regulation of TRIM-21 expression occurs through an ERalpha-dependent mechanism, a pathway that was observed to be overactive in SLE patients. PMID: 24449583 Autoantibodies to the RING domain of Ro52 significantly correlate with disease activity in systemic lupus erythematosus. PMID: 23554036 Our data demonstrate that multiple IRFs tightly regulate expression of Trim21 in immune cells. PMID: 23975864 This retrospective study supports the routine distinction of anti-SSA/Ro60 and anti-Ro52/TRIM21 due to their different clinical associations. PMID: 23039326 Anti-TRIM21 antibodies were the second most common autoantibodies in this systemic sclerosis cohort. PMID: 22394602 Data suggest that the identification of the SS-A/Ro pattern at the ANA-HEp-2 screening routine shall lead to specific tests for the identification of anti-SS-A/Ro antibodies. PMID: 23357050 Intracellular antibody-bound pathogens stimulate immune signaling via the Fc receptor TRIM21. PMID: 23455675 Anti-Ro52 antibodies were closely associated with the main clinical, histopathological and immunological features of primary Sjogren's syndrome. PMID: 22704838 analysis of a novel role for tyrosine phosphorylation in regulating the interaction with IRF3 and the activity of TRIM21 downstream of TLR3 and TLR4 PMID: 22479513 The direct interaction between TRIM21 and neutralizing antibody is essential, as single-point mutations within the TRIM21-binding site in the Fc region of a potently neutralizing antibody impair virus neutralization. PMID: 22647693 data suggest that Ro52/SSA is involved in death receptor-mediated apoptosis by regulating c-FLIP(L) PMID: 22288650 These findings shed light on a new physiological role for Ro52 that is important to intracellular immunity. PMID: 22178074 anti-Ro52 autoantibodies binding the RING domain of Ro52 may be actively involved in the pathogenesis of rheumatic autoimmune disease by inhibiting Ro52-mediated ubiquitination. PMID: 21862588 FADD and TRIM21 together negatively regulate the late IFN-alpha pathway in response to viral infection. PMID: 21183682 60 kD Ro and nRNP A frequently initiate human lupus autoimmunity PMID: 20224770 Cells possess a cytosolic IgG receptor, tripartite motif-containing 21 (TRIM21), which binds to antibodies with a higher affinity than any other IgG receptor in the human body. PMID: 21045130 Results suggest that Ro52-mediated ubiquitination promotes the degradation of IRF7 following TLR7 and TLR9 stimulation. PMID: 20668674 Ro52-mediated monoubiquitination is involved in the subcellular translocation of active IKK beta to autophagosomes. PMID: 20627395 Importantly, the Ro52 cytoplasmic bodies are highly motile and are located along the microtubule network. These results suggest that the Ro52 cytoplasmic bodies are unidentified structures that are transported along the microtubule network. PMID: 20013343 Ro52 down-regulates Tax-induced NF-kappaB signalling by monoubiquitinating IKKbeta and by reducing the level of Tax PMID: 19675099

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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