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  4. Recombinant Human E3 ubiquitin-protein ligase synoviolin (SYVN1), partial

Recombinant Human E3 ubiquitin-protein ligase synoviolin (SYVN1), partial

  • 货号：
    CSB-YP803115HU1
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP803115HU1
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 货号：
    CSB-EP803115HU1-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 货号：
    CSB-BP803115HU1
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP803115HU1
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 别名：
    SYVN1; HRD1; KIAA1810; E3 ubiquitin-protein ligase synoviolin; RING-type E3 ubiquitin transferase synoviolin; Synovial apoptosis inhibitor 1
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Partial
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    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.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation. Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis. Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1. During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells.
  • 基因功能参考文献：
    1. This study showed that Herp stability was regulated by synoviolin through lysine ubiquitination-independent proteasomal degradation. PMID: 29863080
    2. Hrd1 is an E3 ubiquitin ligase in human T cells.IHrd1 expression is increased in CD4-positive T cells from multiple sclerosis patients. PMID: 27417417
    3. PADI4 interacted with SYVN1 directly and that overexpression of PADI4 suppressed the ubiquitination of proteins. Thus, a reduction in ER stress induced by PADI4 may abrogate the initiation of chronic RA by suppressing the proliferative signals of RA synoviocytes. PMID: 29039504
    4. Amyloid beta oligomers modulate BACE1 through an XBP-1-dependent pathway involving HRD1. PMID: 27853315
    5. findings support a model of Hrd1 complex formation, where the Hrd1 cytoplasmic domain and FAM8A1 have a central role in the assembly and activity of this ERAD machinery. PMID: 28827405
    6. HSP70-Hrd1 axis represents a potential therapeutic target for restoring the oncorepressor activity of unstable lymphoma-associated Blimp-1 mutants. PMID: 28842558
    7. this study proved that SYVN1 enhances SERPINA1(E342K)/ATZ degradation through SQSTM1-dependent autophagy and attenuates SERPINA1(E342K)/ATZ cytotoxicity. PMID: 28121484
    8. Results demonstrated that overexpression of Hrd1 increased the proteasomal degradation and microtubule-dependent aggresome formation of OPTN in the microtubular organizing center, whereas knockdown of Hrd1 stabilized OPTN and inhibited aggresome formation of OPTN. PMID: 28334804
    9. Data show that E3 ubiquitin ligase HRD1 (HRD1) decreased the protein level of S100A8 through ubiquitination. PMID: 28423597
    10. Analysis of affinity-captured Hrd1 complexes from these cells by size-exclusion chromatography, immunodepletion, and absolute quantification mass spectrometry identified two major high-molecular-mass complexes with distinct sets of interacting proteins and variable stoichiometries, suggesting a hitherto unrecognized heterogeneity in the functional units of Hrd1-mediated protein degradation. PMID: 28411238
    11. This study provides new knowledge of the CFTR biosynthetic pathway. It suggests that SYVN1 and FBXO2 represent two distinct multiprotein complexes that may degrade DeltaF508-CFTR in airway epithelia and identifies a new role for NEDD8 in regulating DeltaF508-CFTR ubiquitination. PMID: 27756846
    12. Study shows that mir125b is up-regulated in osteoarthritis (OA) and inversely correlated with SYNV1 expression. Also, findings demonstrated that miR- 125b-5p could promote apoptosis of synovial cells through targeting the SYVN1 gene, and the excessive apoptosis of synovial cells could contribute to the development of OA. PMID: 28260078
    13. HRD1 is a novel substrate for USP19. USP19 negatively regulates the ubiquitination of HRD1 and prevents it from undergoing proteasomal degradation. PMID: 27827840
    14. Prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP. PMID: 26740554
    15. OS-9, an ER-resident lectin, acts downstream of Grp94 to further recognize misfolded alpha1 subunits in a glycan-dependent manner. This delivers misfolded alpha1 subunits to the Hrd1-mediated ubiquitination and the valosin-containing protein-mediated extraction pathway. PMID: 26945068
    16. These findings uncover a novel role for HRD1 in breast cancer. PMID: 26536657
    17. The inherently unstable nature of the human SEL1L protein lies in its transmembrane domain, and that association of HRD1 with the SEL1L transmembrane domain restored its stability. PMID: 26471130
    18. specific silencing of Derlin-2, p97 and HRD1 by shRNAs increases steady state levels of proinsulin. these ERAD constituents are critically involved in proinsulin degradation and may therefore also play a role in subsequent antigen generation. PMID: 26107514
    19. Charcot-Marie-Tooth disease-related PMP22 is trapped in the endoplasmic reticulum by calnexin-dependent retention and Rer1-mediated early Golgi retrieval systems and partly degraded by the Hrd1-mediated endoplasmic reticulum-associated degradation system. PMID: 25385046
    20. Results show that HRD1 and RFP2 contributes are required for the disposal of V247M alpha-sarcoglycan mutant. PMID: 24565866
    21. Herp localizes to the endoplasmic reticulum-derived quality control compartment (ERQC) and recruits HRD1, which targets to endoplasmic reticulum associated degradation the substrate presented by the OS-9 lectin at the ERQC. PMID: 24478453
    22. identified Hrd1 as a novel E3 ubiquitin ligase responsible for compromised Nrf2 response during liver cirrhosis PMID: 24636985
    23. a new HRD1-associated membrane protein named HERP2, which is homologous to the previously identified HRD1 partner HERP1. Despite sequence homology, HERP2 is constitutively expressed in cells, whereas HERP1 is highly induced by ER stress. PMID: 24366871
    24. the interactions between P97 and these motifs, including VCP-binding motif (VBM) and VCP-interacting motif (VIM). The solution structures of the VBM motif from HRD1 and the VIM motif from SVIP are both comprised mainly of a single alpha-helix. PMID: 24100225
    25. derlin2 functions with HRD1 in ERAD of certain substrates independent of their glycosylation status. PMID: 23867461
    26. subset of integral membrane proteins, therefore, requires an early dislocation event to expose part of their luminal domain to the cytosol, before HRD1-mediated polyubiquitination and dislocation PMID: 23929775
    27. Synoviolin up-regulates amyloid beta production by targeting a negative regulator of gamma-secretase, Rer1, for degradation. PMID: 23129766
    28. Hrd1 functions as an E3 targeting tau or abnormal p-tau for proteasome degradation. PMID: 22280354
    29. regulation of the stability and assembly of the HRD1-SEL1L complex is critical to optimize the degradation kinetics of ERAD substrates PMID: 21454652
    30. binding of Herp to Hrd1-containing ERAD complexes positively regulates the ubiquitylation activity of these complexes, thus permitting survival of the cell during ER stress. PMID: 21149444
    31. data support a physiological role for HRD1 and UBE2J1 in the homeostatic regulation of MHC class I assembly and expression PMID: 21245296
    32. Using brain tissue from Alzheimer's disease and normal subjects, a negative correlation was found between the expressed levels of HRD1 and of amyloid-beta; this suggests the possible involvement of HRD1 in amyloid-beta generation. PMID: 20606367
    33. serine-dependent, HRD1-mediated ubiquitination targets TCRalpha to the ERAD pathway PMID: 20519503
    34. HRD1 promotes ubiquitination and degradation of amyloid precursor protein (APP) that leads to decreased amyloid beta production, whereas HRD1 loss in Alzheimer's disease leads to accumulation of APP and increased levels of amyloid beta. PMID: 20237263
    35. These data demonstrate a role of the E3 ubiquitin ligases in CTA1 retro-translocation. PMID: 19864457
    36. The results support that gp78 is an E3 targeting CFTRDeltaF508 for degradation and Hrd1 inhibits CFTRDeltaF508 degradation by acting as an E3 for gp78. PMID: 19828134
    37. HRD1 protects against endoplasmic reticulum stress-induced apoptosis through endoplasmic reticulum-associated degradation. PMID: 12459480
    38. endogenous hHrd1 resides in the ER and has a ubiquitin-ligase activity PMID: 12646171
    39. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum PMID: 14593114
    40. Results showed that Synoviolin, a novel causative factor for rheumatoid arthritis, is up-regulated in proliferating synovial cells in the disease. PMID: 16786162
    41. Elevated peripheral blood (PB) levels of synoviolin were associated with nonresponse to infliximab treatment. Upregulation of synoviolin by IL-lbeta and TNFalpha may contribute to prolonged survival of immune cells and rheumatoid arthritis chronicity. PMID: 16802346
    42. These results suggest that Hrd1 is a novel htt-interacting protein that can target pathogenic httN for degradation and is able to protect cells against httN-induced cell death. PMID: 17141218
    43. the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin' destroys p53 PMID: 17170702
    44. endoplasmic reticulum stress-induced HRD1 and SEL1 expressions are mediated by IRE1-XBP1- and ATF6-dependent pathways, respectively PMID: 17967421
    45. overexpressed in the synovial cells of patients with rheumatoid arthritis, resulting in a state in which the cell deals with accumulated unfolded proteins excessively PMID: 18235538
    46. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD PMID: 18264092
    47. These findings reveal a role for SEL1L and HRD1 in IgM quality control. PMID: 18314878
    48. proline-rich domain of HRD1 is necessary to promote the degradation of Pael-R and that the protein's transmembrane domain is necessary to transfer Pael-R from the endoplasmic reticulum (ER) to the cytosol. PMID: 18344614
    49. XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP PMID: 18502753
    50. analysed the promoter of human HRD1, which encodes an E3 ubiquitin ligase, an important component of ERAD PMID: 18664523

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  • 亚细胞定位：
    Endoplasmic reticulum membrane; Multi-pass membrane protein.
  • 蛋白家族：
    HRD1 family
  • 组织特异性：
    Ubiquitously expressed, with highest levels in liver and kidney (at protein level). Up-regulated in synovial tissues from patients with rheumatoid arthritis (at protein level).
  • 数据库链接：

    HGNC: 20738

    OMIM: 608046

    KEGG: hsa:84447

    STRING: 9606.ENSP00000366395

    UniGene: Hs.75859