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  4. Recombinant Human E3 ubiquitin-protein ligase SMURF2 (SMURF2)

Recombinant Human E3 ubiquitin-protein ligase SMURF2 (SMURF2)

  • 中文名稱(chēng)：
    人SMURF2重組蛋白
  • 貨號(hào)：
    CSB-BP872532HU
  • 規(guī)格：
  • 來(lái)源：
    Baculovirus
  • 其他：
  • 中文名稱(chēng)：
    人SMURF2重組蛋白
  • 貨號(hào)：
    CSB-EP872532HU-B
  • 規(guī)格：
  • 來(lái)源：
    E.coli
  • 共軛：
    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：
  • 中文名稱(chēng)：
    人SMURF2重組蛋白
  • 貨號(hào)：
    CSB-MP872532HU
  • 規(guī)格：
  • 來(lái)源：
    Mammalian cell
  • 其他：

產(chǎn)品詳情

  • 純度：
    Greater than 85% as determined by SDS-PAGE.
  • 基因名：
    Name:SMURF2
  • Uniprot No.：
  • 別名：
    E3 ubiquitin-protein ligase SMURF2; EC 6.3.2.; hSMURF2; MGC138150; Smad specific E3 ubiquitin ligase 2; SMAD specific E3 ubiquitin protein ligase 2; SMAD ubiquitination regulatory factor 2; SMAD-specific E3 ubiquitin-protein ligase 2; SMUF2_HUMAN; Smurf2; Ubiquitin protein ligase SMURF2
  • 種屬：
    Homo sapiens (Human)
  • 蛋白長(zhǎng)度：
    full length protein
  • 表達(dá)區(qū)域：
    1-748
  • 氨基酸序列
    MSNPGGRRNG PVKLRLTVLC AKNLVKKDFF RLPDPFAKVV VDGSGQCHST DTVKNTLDPK WNQHYDLYIG KSDSVTISVW NHKKIHKKQG AGFLGCVRLL SNAINRLKDT GYQRLDLCKL GPNDNDTVRG QIVVSLQSRD RIGTGGQVVD CSRLFDNDLP DGWEERRTAS GRIQYLNHIT RTTQWERPTR PASEYSSPGR PLSCFVDENT PISGTNGATC GQSSDPRLAE RRVRSQRHRN YMSRTHLHTP PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLSN INCEELGPLP PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNR QNQLKDQQQQ QVVSLCPDDT ECLTVPRYKR DLVQKLKILR QELSQQQPQA GHCRIEVSRE EIFEESYRQV MKMRPKDLWK RLMIKFRGEE GLDYGGVARE WLYLLSHEML NPYYGLFQYS RDDIYTLQIN PDSAVNPEHL SYFHFVGRIM GMAVFHGHYI DGGFTLPFYK QLLGKSITLD DMELVDPDLH NSLVWILEND ITGVLDHTFC VEHNAYGEII QHELKPNGKS IPVNEENKKE YVRLYVNWRF LRGIEAQFLA LQKGFNEVIP QHLLKTFDEK ELELIICGLG KIDVNDWKVN TRLKHCTPDS NIVKWFWKAV EFFDEERRAR LLQFVTGSSR VPLQGFKALQ GAAGPRLFTI HQIDACTNNL PKAHTCFNRI DIPPYESYEK LYEKLLTAIE ETCGFAVE
  • 蛋白標(biāo)簽：
    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.
  • 產(chǎn)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.
  • 復(fù)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.
  • 儲(chǔ)存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)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.
  • 貨期：
    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.
  • 注意事項(xiàng)：
    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.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

  • 功能：
    E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby downregulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation.; (Microbial infection) In case of filoviruses Ebola/EBOV and Marburg/MARV infection, the complex formed by viral matrix protein VP40 and SMURF2 facilitates virus budding.
  • 基因功能參考文獻(xiàn)：
    1. High SMURF2 expression is associated with breast cancer progression. PMID: 29534682
    2. Smurf2, an E3 ubiquitin ligase, interacts with PDE4B and attenuates liver fibrosis through miR-132 mediated CTGF inhibition. PMID: 29100790
    3. Low SMURF2 expression is associated with breast cancer organoid invasiveness. PMID: 28423498
    4. Results identified Smurf2 as an essential regulator of Topo IIalpha, providing novel insights into its control and into the suggested tumor-suppressor functions of Smurf2. PMID: 28611047
    5. found that phospho-AIMP2 dissociated from the multi-tRNA synthetase complex and translocated to the nucleus, where it bound to Smurf2 PMID: 27197155
    6. Ectopic expression of human Smurf2 driven by the Col2a1 promoter accelerated disc degeneration in Col2a1-Smurf2 transgenic mice, and that higher levels of connective tissue growth factor protein and mRNA were present in Col2a1-Smurf2 transgenic discs, indicate that Smurf2 accelerates disc degeneration via upregulation of connective tissue growth factor. PMID: 28387615
    7. data suggest for the first time that the choice of binding partners for SMURF2 can sustain or repress TGFbeta signaling, and RNF11 may promote TGFbeta-induced cell migration. PMID: 28292929
    8. Neddylation of Smurf1 activates its ubiquitin ligase activity and Smurf2 exerts Nedd8 ligase activity. This study provided new clues of Smurf2 activation regulation. PMID: 27086113
    9. The Smurf2 acts in a sumoylation-regulated manner to suppress TGFbeta-induced Epithelial-mesenchymal transition. PMID: 26679521
    10. the findings of this study demonstrate that the downregulation of SnoN expression in hRPTECs under high-glucose conditions is mediated by the increased expression of Smurf2 through the TGF-b1/Smad signaling pathway. PMID: 26743567
    11. SMURF2 is a critical target of USP15 in the TGF-beta signaling pathway. PMID: 26435193
    12. Data show that miR15b mediates SMURF2 expression in pancreatic cancer and suggest miR15b as an oncogene by promoting epithelial-mesenchymal transition and SMURF2 as a tumor suppressor gene which expression is inhibited by miR15b in pancreatic cancer. PMID: 26166038
    13. Methylation by PRMT1 may regulate Smurf2 stability and control TGF-beta signaling. PMID: 26126536
    14. Studies on Smurf2 and Nedd4 show that the C2 domain has the potential to regulate E3 activity by maintaining the HECT domain in a low-activity state where its ability for transthiolation and noncovalent Ubiquitin binding are impaired. PMID: 25438670
    15. miR-424 regulates the myofibroblast differentiation during epithelial-to-mesenchymal transition by potentiating the TGF-beta signaling pathway, likely through Smurf2. PMID: 25524739
    16. The SMURF2:UBCH5 complex is critical in maintaining KRAS protein stability. PMID: 24709419
    17. These results suggest a novel regulatory mechanism for YY1 function by Smurf2. PMID: 24803334
    18. Provide evidence of posttranscriptional downregulation of Smurf2 in triple-negative breast cancers, and demonstrate that the loss of RB function is involved in microRNA-mediated interference with Smurf2 translation. PMID: 24485087
    19. Smurf2 mediates ubiquitination and degradation of YY1, a key germinal centre transcription factor. PMID: 24121673
    20. This study showed that, by targeting SMURF2, NS3-4A appears to block the negative regulation of TGF-beta signaling, increasing the responsiveness of cells to TGF-beta. PMID: 23781096
    21. Smurf2-mediated degradation of EZH2 enhances neuron differentiation and improves functional recovery after ischaemic stroke. PMID: 23526793
    22. Depleting SMURF2 reduced MITF expression and substantially lowered the threshold for MEK inhibitor-induced apoptosis, and sensitized melanoma cells to the cytotoxic effects of selumetinib. PMID: 23250956
    23. Smurf2 interacts with Smad7 to suppress TGF-beta-mediated liver fibrosis through the ubiquitin-dependent degradation of TbetaRI during the early period of liver fibrosis. PMID: 22624557
    24. TGFbeta induces expression of Smad7, Smurf2, and SIK1, the products of which physically and functionally interlink to control the activity of this pathway. PMID: 22378783
    25. tumor suppression function that maintains genomic stability by control of the epigenetic landscape of histone modifications through RNF20 PMID: 22231558
    26. mediates degradation of ubiquitinated HSP27 through the ubiquitin-proteasome pathway PMID: 21967197
    27. SMURF2 is a novel E3 ubiquitin ligase for KLF5 and negatively regulates KLF5 by targeting it for proteasomal degradation. PMID: 21953463
    28. RLIM directly binds to Smurf2, enhancing TGF-beta responsiveness in osteosarcoma U2OS cells. PMID: 21945933
    29. SMURF2-mediated protective ubiquitination of EGFR may be responsible for EGFR overexpression in certain tumors. PMID: 21750651
    30. These findings suggest that Smurf2 plays a significant role in the pathomechanism of progressive supranuclear palsy PMID: 20819168
    31. Inhibition of Smad signaling may be achieved at the transcriptional level through c-Ski/receptor-Smad/co-mediator Smad4 interactions--REVIEW PMID: 19898560
    32. Smurf2 recruits the Rb and p53 pathways for induction of cellular replicative senescence. PMID: 15574587
    33. SMURF2 ubiquitin ligase is transcriptionally induced by TGFbeta. PMID: 15862290
    34. A 2.1 A resolution X-ray crystal structure of the Smurf2 HECT domain reveals that it has a suboptimal E2 binding pocket that could be optimized by mutagenesis. PMID: 16061177
    35. analysis of the WW domain recognition motif for the interaction of Smad7 and the E3 ubiquitin ligase Smurf2 PMID: 16641086
    36. Autoinhibition of the HECT-type ubiquitin ligase SMURF2 through its C2 domain. PMID: 17719543
    37. Ectopic expression of Smurf2 driven by the Col2a1 promoter accelerated the process of endochondral ossification including chondrocyte maturation and osteoblast differentiation through upregulation of beta-catenin PMID: 18052755
    38. Smurf2 action may be a useful strategy for inhibition of cancer cell growth. PMID: 18181147
    39. dysregulation of Smurf2 could contribute to an aberrant TGF-beta/Smad signaling in the pathogenesis of kidney fibrosis PMID: 18353873
    40. A significant elevation in expression of SMURF2 in oral squamous cell carcinoma cells was seen in carbon and neon-irradiated cells. PMID: 18514338
    41. These results suggest an important role for Smurf2 binding to TRAF2 in determining specific signalling outputs of TNF-R2. PMID: 18671942
    42. Smurf2 is up-regulated during Osteoarthritis in humans PMID: 18821706
    43. Inhibition of PI3K or mTOR reduced the level of Rap1B, which acts downstream of Rheb and mTOR. The ubiquitin E3 ligase Smurf2 mediates the restriction of Rap1B by initiating its degradation. PMID: 18842593
    44. Smurf2 regulates the localization and stability of Mad2. PMID: 18852296
    45. Pin1 negatively regulates TGF-beta signaling by down-regulating Smad2/3 protein levels via induction of Smurf2-mediated ubiquitin-proteasomal degradation. PMID: 19122240
    46. Results establish an important role for Smurf2 in breast cancer progression and indicate that Smurf2 is a novel regulator of breast cancer cell migration and invasion. PMID: 19155312
    47. Smurf2 promotes trophoblast cell migration and invasion, and this function may involve downregulation of TGF-beta type I receptor. PMID: 19255252
    48. Smurf2-mediated upregulation of beta-catenin through induction of proteasomal degradation of GSK-beta in chondrocytes may activate articular chondrocyte maturation and associated alteration of gene expression, the early events of osteoarthritis. PMID: 19481076
    49. Data show that REDD1 is subject to ubiquitin-mediated degradation mediated by the CUL4A-DDB1-ROC1-beta-TRCP E3 ligase complex and through the activity of glycogen synthase kinase 3beta. PMID: 19557001
    50. E3 ubiquitin-protein ligase constitutive photomorphogenesis protein 1 is needed for COP1 for degradation via the ubiquitin-proteasome pathway. PMID: 19805145

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  • 亞細(xì)胞定位：
    Nucleus. Cytoplasm. Cell membrane. Membrane raft. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.
  • 組織特異性：
    Widely expressed.
  • 數(shù)據(jù)庫(kù)鏈接：

    HGNC: 16809

    OMIM: 605532

    KEGG: hsa:64750

    STRING: 9606.ENSP00000262435

    UniGene: Hs.515011