Recombinant Human E3 Ubiquitin-Protein Ligase Smurf1 (SMURF1) Protein (His)

Name: Recombinant Human E3 Ubiquitin-Protein Ligase Smurf1 (SMURF1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07149P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human E3 Ubiquitin-Protein Ligase Smurf1 (SMURF1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9HCE7
Target Symbol	SMURF1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	VESPSQDQRLQAQRLRNPDVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPSGTIPGGDAAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLPLPSEGSLEDEELPAQRY
Expression Range	198-374aa
Protein Length	Partial
Mol. Weight	24.1 kDa
Research Area	Cell Biology
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 that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS. Plays a role in dendrite formation by melanocytes.
Subcellular Location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Database References	HGNC: 16807 OMIM: 605568 KEGG: hsa:57154 STRING: 9606.ENSP00000354621 UniGene: PMID: 28169289 Expression of Smurf1 was increased with WHO grade and was consistent with poor prognosis of gliomas. PMID: 28321604 Smurf1 interacts with and targets Securin, an inhibitor of sister-chromatid separation, for poly-ubiquitination and proteasomal degradation. PMID: 28658604 Smurf1 overexpression decreases USP25 protein turnover, and the E3 ligase enzymatic activity of Smurf1 is required for USP25 degradation. PMID: 29518389 SMURF1 can be potentially used as a clinical biomarker and target for novel treatment of human GC. PMID: 28731194 Uev1A appears to be involved in the BMP signaling pathway in which it collaborates with a ubiquitin E3 ligase Smurf1 to promote Smad1 degradation in a Ubc13-independent manner. PMID: 28771228 High smurf1 expression is associated with neoplasms. PMID: 27036023 activation of AMPK upregulated Smad6 and Smurf1 and thereby enhanced their interactions, resulting in its proteosome-dependent degradation of ALK2. PMID: 28847510 we propose that the PKA-Smurf1-PIPKIgamma pathway has an important role in pulmonary tumorigenesis and imposes substantial clinical impact on development of novel diagnostic markers and therapeutic targets for lung cancer treatment. PMID: 28581524 SMURF1 is increased in patients with pulmonary arterial hypertension PMID: 27214554 Data suggest that SMURF1 is required for S phase progression; SMURF1 promotes ubiquitination-dependent degradation of WEE1; these functions of SMURF1 appear to be linked and may be important in cell proliferation and tumorigenesis. (SMURF1 = SMAD specific E3 ubiquitin protein ligase 1; WEE1 = wee 1 homolog [S pombe] protein) PMID: 28294307 Taken together, our study for the first time clarified that the E3 ligase Smurf1 regulates USP5 protein stability and USP5-mediated TNF-alpha production through the ubiquitin proteasome pathway. PMID: 27133717 results reveal the regulatory circuit between RUNX2 and SMURF1 controls RUNX2 expression and regulates odntoblastic differentiation in hDPSCs. PMID: 25260729 EGF/Smurf1 inhibits Wnt/beta-catenin-induced osteogenic differentiation and that Smurf1 downregulates Wnt/b-catenin signaling by enhancing proteasomal degradation of beta-catenin. PMID: 26015066 a model that CD166 regulates MCAM through a signaling flow from activation of PI3K/AKT and c-Raf/MEK/ERK signaling to the inhibition of potential MCAM ubiquitin E3 ligases, betaTrCP and Smurf1. PMID: 26004137 SND1 promoted expression of the E3 ubiquitin ligase Smurf1, leading to RhoA ubiquitination and degradation. PMID: 25596283 NF-kappaB bind to the -411 to -420 region of the SMURF1 promoter and plays an essential role in the expression of SMURF1. PMID: 26252093 Smurf1 determines cell apoptosis rates downstream of DNA damage-induced ATR/Chk1 signalling by promoting degradation of RhoB. PMID: 25249323 The role of SMURF1 and inhibition of BMP signaling in maintaining a CSC-like population was confirmed by the loss of a CD44(high) expressing. PMID: 25471937 Results suggest that elevated transcription and expression levels of ubiquitin ligase E3s WWP1, Smurf1 and Smurf2 genes may be the mechanisms of occurrence, development and metastasis of prostate cancer. PMID: 25051198 Fbxo3 promotes the proteasomal degradation of Smurf1. Fbxo3 promotes the poly-ubiquitination of Smurf1. PMID: 25721664 TRIB2 associated-ubiquitin E3 ligases beta-transducin repeat-containing E3 ubiquitin protein ligase (beta-TrCP), COP1 and Smad ubiquitination regulatory factor 1 (Smurf1) reduced TCF4/beta-Catenin expression, and these effects could be enhanced by TRIB2. PMID: 25311538 association of cortactin with Pfn-1 is regulated by c-Abl-mediated cortactin phosphorylation PMID: 24700460 Smurf1 is localized within the Hirano bodies of Alzheimer's disease brains. PMID: 24238996 CKIP-1 controlled Smurf1 expression in colon cancer PMID: 23995790 Inhibiting Smurf1 mediated ubiquitination of Smad1/5. PMID: 24828823 Results suggest that EGF-induced SMURF1 plays a role in breast cancer cell migration and invasion through the downregulation of RhoA. PMID: 24241683 impaired phosphorylation and ubiquitination by p70S6K and Smurf1 increase the protein stability of TRIB2 in liver cancer PMID: 24089522 Data indicate that Smad ubiquitin regulatory factor Smurf1 regulates cell migration through ubiquitination of tumor necrosis factor receptor-associated factor 4 (TRAF4). PMID: 23760265 Resistance exercise resulted in a significant downregulation of MSTN and FBXO32 mRNA expression and a significant upregulation in FSTL3 and SMURF1 mRNA expression, and carbohydrate and protein feeding have little influence on the these markers expression. PMID: 22476926 Smurf1 turnover is mediated by Ckip-1 and Rpt6. PMID: 23032291 The expression of SMURF1 is enhanced in hepatocellular carcinoma, which may have played a role in the disease through affecting apoptosis and proliferation of hepatic cancer cells. PMID: 23042388 USP9X is an important regulatory protein of SMURF1. PMID: 23184937 Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing E3 ligase Smurf1-mediated MAVS degradation. PMID: 23087404 A Cdh1-APC/Smurf1/RhoA pathway that mediates axonal growth suppression in the developing mammalian brain. PMID: 22949615 Smurf1 is a negative feedback regulator for IFN-gamma signaling by targeting STAT1 for ubiquitination and proteasomal degradation. PMID: 22474288 Inflammatory cytokines led to direct activation of Smurf1 and downregulation of miR-17, thereby increasing degradation of Smurf1-mediated osteoblast-specific factors. PMID: 21898695 studies uncover a cell-cycle-independent function of Cdh1, establishing Cdh1 as an upstream component that governs Smurf1 activity PMID: 22152476 SMURF1 is an amplified oncogene driving multiple tumorigenic phenotypes in pancreatic cancer PMID: 21887346 Data report that the C2 domain of Smurf1 is necessary and sufficient for binding RhoA, and therefore is crucial for targeting RhoA for ubiquitination. PMID: 21708152 ER stress induces Smurf1 degradation and WFS1 up-regulation PMID: 21454619 the Smurf1 C2 domain has a role in substrate selection and cellular localization PMID: 21402695 This study provided the first evidence that Smurf1 functions as an E3 ligase to promote the ubiquitination and proteasomal degradation of KLF2. PMID: 21382345 These results suggest a new role of Smurf1 in inflammation and immunity through controlling the degradation of TRAFs. PMID: 19937093 plasma membrane localization of Smad7 by Smurf1 requires the C2 domain of Smurf1 and is essential for the inhibitory effect of Smad7 in the transforming growth factor-beta signaling pathway PMID: 12151385 CRM1-dependent nuclear export of Smurf1 is essential for the negative regulation of TGF-beta signaling by Smad7. PMID: 12519765 Smurf1 links the Cdc42/Rac1-PAR6 polarity complex to degradation of RhoA in lamellipodia and filopodia to prevent RhoA signaling during dynamic membrane movements PMID: 14657501 Smad7 and Smurf1 have roles in regulation of TGF-beta signaling in scleroderma fibroblasts PMID: 14722617 rhoA GTP-Binding Protein is targeted for ubiquitination and degradation via Smurf1 PMID: 15710384 Smad6 interacts with Runx2 and mediates Smad ubiquitin regulatory factor 1-induced Runx2 degradation PMID: 16299379

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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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