Recombinant Human E3 Ubiquitin-Protein Ligase Smurf2 (SMURF2) Protein (His)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Smurf2 (SMURF2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-05068P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Smurf2 (SMURF2) 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	Q9HAU4
Target Symbol	SMURF2
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE
Expression Range	1-748aa
Protein Length	Full Length
Mol. Weight	90.3 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.
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 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.
Subcellular Location	Nucleus. Cytoplasm. Cell membrane. Membrane raft. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.
Database References	HGNC: 16809 OMIM: 605532 KEGG: hsa:64750 STRING: 9606.ENSP00000262435 UniGene: PMID: 29534682 Smurf2, an E3 ubiquitin ligase, interacts with PDE4B and attenuates liver fibrosis through miR-132 mediated CTGF inhibition. PMID: 29100790 Low SMURF2 expression is associated with breast cancer organoid invasiveness. PMID: 28423498 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 found that phospho-AIMP2 dissociated from the multi-tRNA synthetase complex and translocated to the nucleus, where it bound to Smurf2 PMID: 27197155 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 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 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 The Smurf2 acts in a sumoylation-regulated manner to suppress TGFbeta-induced Epithelial-mesenchymal transition. PMID: 26679521 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 SMURF2 is a critical target of USP15 in the TGF-beta signaling pathway. PMID: 26435193 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 Methylation by PRMT1 may regulate Smurf2 stability and control TGF-beta signaling. PMID: 26126536 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 miR-424 regulates the myofibroblast differentiation during epithelial-to-mesenchymal transition by potentiating the TGF-beta signaling pathway, likely through Smurf2. PMID: 25524739 The SMURF2:UBCH5 complex is critical in maintaining KRAS protein stability. PMID: 24709419 These results suggest a novel regulatory mechanism for YY1 function by Smurf2. PMID: 24803334 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 Smurf2 mediates ubiquitination and degradation of YY1, a key germinal centre transcription factor. PMID: 24121673 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 Smurf2-mediated degradation of EZH2 enhances neuron differentiation and improves functional recovery after ischaemic stroke. PMID: 23526793 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 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 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 tumor suppression function that maintains genomic stability by control of the epigenetic landscape of histone modifications through RNF20 PMID: 22231558 mediates degradation of ubiquitinated HSP27 through the ubiquitin-proteasome pathway PMID: 21967197 SMURF2 is a novel E3 ubiquitin ligase for KLF5 and negatively regulates KLF5 by targeting it for proteasomal degradation. PMID: 21953463 RLIM directly binds to Smurf2, enhancing TGF-beta responsiveness in osteosarcoma U2OS cells. PMID: 21945933 SMURF2-mediated protective ubiquitination of EGFR may be responsible for EGFR overexpression in certain tumors. PMID: 21750651 These findings suggest that Smurf2 plays a significant role in the pathomechanism of progressive supranuclear palsy PMID: 20819168 Inhibition of Smad signaling may be achieved at the transcriptional level through c-Ski/receptor-Smad/co-mediator Smad4 interactions--REVIEW PMID: 19898560 Smurf2 recruits the Rb and p53 pathways for induction of cellular replicative senescence. PMID: 15574587 SMURF2 ubiquitin ligase is transcriptionally induced by TGFbeta. PMID: 15862290 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 analysis of the WW domain recognition motif for the interaction of Smad7 and the E3 ubiquitin ligase Smurf2 PMID: 16641086 Autoinhibition of the HECT-type ubiquitin ligase SMURF2 through its C2 domain. PMID: 17719543 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 Smurf2 action may be a useful strategy for inhibition of cancer cell growth. PMID: 18181147 dysregulation of Smurf2 could contribute to an aberrant TGF-beta/Smad signaling in the pathogenesis of kidney fibrosis PMID: 18353873 A significant elevation in expression of SMURF2 in oral squamous cell carcinoma cells was seen in carbon and neon-irradiated cells. PMID: 18514338 These results suggest an important role for Smurf2 binding to TRAF2 in determining specific signalling outputs of TNF-R2. PMID: 18671942 Smurf2 is up-regulated during Osteoarthritis in humans PMID: 18821706 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 Smurf2 regulates the localization and stability of Mad2. PMID: 18852296 Pin1 negatively regulates TGF-beta signaling by down-regulating Smad2/3 protein levels via induction of Smurf2-mediated ubiquitin-proteasomal degradation. PMID: 19122240 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 Smurf2 promotes trophoblast cell migration and invasion, and this function may involve downregulation of TGF-beta type I receptor. PMID: 19255252 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 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 E3 ubiquitin-protein ligase constitutive photomorphogenesis protein 1 is needed for COP1 for degradation via the ubiquitin-proteasome pathway. PMID: 19805145

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.