Recombinant Human Sentrin-specific protease 1(SENP1)

Code CSB-YP885787HU
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Source Yeast
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Code CSB-EP885787HU
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Source E.coli
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Code CSB-EP885787HU-B
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Source E.coli
Conjugate 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.
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Code CSB-BP885787HU
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Source Baculovirus
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Code CSB-MP885787HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names SENP1
Uniprot No. Q9P0U3
Alternative Names SENP 1; SENP1; SENP1_HUMAN; Sentrin specific protease 1; Sentrin-specific protease 1; Sentrin/SUMO specific protease 1; Sentrin/SUMO specific protease; Sentrin/SUMO specific protease SENP 1; Sentrin/SUMO specific protease SENP1; Sentrin/SUMO-specific protease SENP1; SUMO1/sentrin specific peptidase 1; SUMO1/sentrin specific protease 1; SuPr 2; SuPr2
Species Homo sapiens (Human)
Expression Region 1-644
Target Protein Sequence MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGHLDRSFTC STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD SRARERLRQI EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV TVVQETQKKG HKLTDSEDEF PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL TITRKDIQTL NHLNWLNDEI INFYMNMLME RSKEKGLPSV HAFNTFFFTK LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD FRKKNITYYD SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL
Protein Length full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
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.
Form 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.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution 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.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life 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.
Lead Time 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.
Notes 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.

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Target Background

Function
Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1. Deconjugates SUMO1 from METTL3. Desumoylates CCAR2 which decreases its interaction with SIRT1. Deconjugates SUMO1 from GPS2.
Gene References into Functions
  1. Results in this present study showed that SENP1 was a risk factor for poor non-small cell lung cancer prognosis. And also demonstrated that the overexpression of SENP1 in non-small cell lung cancer was related to chemotherapy resistance. PMID: 30043429
  2. SENP1 is a crucial c-Myc deSUMOylating enzyme that positively regulates c-Myc's stability and activity. PMID: 30305424
  3. endothelial SENP1-mediated SUMOylation drives graft arteriosclerosis by regulating the synergistic effect of GATA2 and NF-kappaB and consequent endothelial dysfunction. PMID: 28569748
  4. Results showed that the expression of SENP1 was remarkably upregulated in osteosarcoma cells (OS) cells. SENP1 positively regulated HIF-1alpha expression level in the setting of hypoxic; subsequently, its depletion markedly ameliorated VEGF production triggered by hypoxia. PMID: 28796315
  5. These results suggest that the miR-133a-3p-SENP1 axis might play a role in cell proliferation and cell cycle regulation of colorectal cancer cells. PMID: 28748780
  6. Despite the requirement of all three nucleoporins for accurate NHEJ, only Nup153 is needed for proper nuclear import of 53BP1 and SENP1-dependent sumoylation of 53BP1. Data support the role of Nup153 as an important regulator of 53BP1 activity and efficient NHEJ. PMID: 28576968
  7. miR-185 was significantly downregulated in RCC tissues and cell lines. SENP1 was a direct target of miR-186, and SENP1 mRNA expression was reversely correlated with miR-186 in RCC tissues. PMID: 28550686
  8. Treatment of cells with streptonigrin resulted in increased global SUMOylation levels and reduced level of hypoxia inducible factor alpha (HIF1alpha). These findings inform both the design of SENP1 targeting strategy and the modification of streptonigrin to improve its efficacy for possible future clinical use. PMID: 29481054
  9. SENP1 promotes cell proliferation and disease progression in clear cell renal cell carcinoma, possibly through deSUMOylating and stabilizing HIF-1alpha, leading to increased expression of key glycolytic enzymes and enhanced glycolytic flux. PMID: 27741516
  10. Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region. PMID: 27576863
  11. GATA1 is an essential downstream target of SENP1 and that the differential expression and response of GATA1 and Bcl-xL are a key mechanism underlying chronic mountain sickness pathology. PMID: 27821551
  12. miRNA1236 regulates hypoxia-induced epithelial-mesenchymal transformation and metastasis by repressing HDAC3 and SENP1 expression. PMID: 27177472
  13. SENP1 deSUMOylated SMAD4 to promote EMT via up-regulating E-cadherin in prostate cancer cells. Therefore, SENP1 is a potential target for treatment of advanced prostate cancer. PMID: 28417919
  14. The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence. PMID: 27178176
  15. this study elucidated that SENP1 is essential for triple-negative breast cancer cell proliferation and migration in vitro, as well as tumor formation and metastasis in vivo PMID: 27573572
  16. Hepatocellular carcinoma cells express a high level of Senp1 which is induced by HGF/c-Met signals. Senp1 silencing reduces the HGF-induced proliferation and migration of HCC cells, induces HCC cell apoptosis and growth arrest, and epithelial-to-mesenchymal transition, with increase of E-cadherin and ZO-1 expression, decrease of fibronectin and N-cadherin expression. PMID: 26695141
  17. a significant role of SENP1 in the regulation of cell migration and invasion in neuroblastoma PMID: 25816890
  18. A key role for SENP1 in astrocytoma development and apoptosis.SENP1 inhibition promotes cell apoptosis by regulating NF-kappa B/Akt signaling pathways. PMID: 27693211
  19. Genetic interactions of SNPs in CARD14, SENP1 and VEGFA might represent a functional mechanism in the pathogenesis of high altitude polycythemia. PMID: 26852650
  20. SENP1 desensitizes hypoxic ovarian cancer cells to cisplatin by up-regulating HIF-1alpha PMID: 26548925
  21. SENP1 expression has strong prognostic impact in a molecularly defined subset of cancers. This is per se not surprising as the biologic impact of each individual molecular event is likely to be dependent on its cellular environment. PMID: 26202067
  22. SENP1 was expressed in human islets, and its mRNA level was unchanged in islets from donors with T2D. In cultured islets, overexpressed SENP1-GFP colocalized with secretory granules at the plasma membrane PMID: 26389676
  23. SENP1 uses remote substrate binding for conformational flexibility and activation PMID: 25263960
  24. SENP1 up-regulation in diseased heart is mediated via calcineurin-NFAT/MEF2C-PGC-1alpha pathway. PMID: 25446185
  25. Over-expression of small ubiquitin-like modifier proteases 1 predicts chemo-sensitivity and poor survival in non-small cell lung cancer.( PMID: 25430449
  26. low expression of miR-145 was correlated with high expression of SENP1 in Prostate cancer cell line and the SENP1 3'-untranslated region was a regulative target of miR-145 in vitro. PMID: 25645686
  27. results delineate a key role for Senp1in IL-6 induced proliferation and survival of MM cells, suggesting it may be a potential new therapeutic target in MM PMID: 25791478
  28. SENP1 deficiency exacerbates ischemia-reperfusion injury in cardiomyocytes via a HIF1alpha-dependent pathway. PMID: 25082844
  29. SENP1 was upregulated in PDAC tissues; overexpressed SENP1 was associated with lymph node metastasis and TNM stage. PMID: 25217324
  30. Data suggest that up-regulation of SENP1 down-regulates insulin secretion and impairs intracellular calcium signaling in islet beta-cells; this secretory dysfunction is due to SENP1-induced apoptosis of islet beta-cells. PMID: 25139051
  31. our data demonstrate that the miR-138/SENP1 cascade is relative to radiosensitization in lung cancer cells and is a potential radiotherapy target. PMID: 24691972
  32. cadmium-induction enhances AR transcriptional activity by decreasing AR SUMOylation PMID: 25014244
  33. Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted. PMID: 24196834
  34. Data suggest that small ubiquitin-like modifier (SUMO)-specific protease 1 (SENP1) expression might contribute to the malignant progression of prostate cancer and as a potential prognostic factor for biochemical recurrence after prostatectomy. PMID: 23089540
  35. Chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis; SENP1 and SENP2 are important mediators of this control. PMID: 24048451
  36. The SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance. PMID: 22688647
  37. Results show the contribution of SENP1 to the progression of prostate cancer, and suggest that SENP1 may be a prognostic marker. PMID: 22733136
  38. A critical role for SENP1-mediated desumoylation in promoting Pin1 function during tumorigenesis. PMID: 23633483
  39. Data show that the loss of OCT4 expression under hypoxia can be triggered by sumoylation, which was regulated by the SUMO1 peptidase SENP1. PMID: 23002208
  40. mutation of K364 to arginine (R) or deSumoylation by small ubiquitin-like modifier (Sumo)-specific protease-1, a nuclear deSumoylase, enhanced the transactivation capacity of LEDGF and its cellular abundance PMID: 22748127
  41. de-SUMOylation is essential for SENP1 modulating XBP1 transcriptional activity. PMID: 22370484
  42. SENP1 might play a role in cell cycle regulation of colon cancer cells PMID: 21669491
  43. crystal structure of human SENP1 was redetermined at 2.4 A degrees resolution with Rwork and Rfree values of 23.1% and 31.3%, respectively PMID: 21505236
  44. Could use the urinary hTERT, SENP1, PPP1CA, and MCM5 mRNA to detect bladder cancer recurrence. PMID: 21106093
  45. Induction of SENP1 in endothelial cells contributes to hypoxia-driven VEGF expression and angiogenesis. PMID: 20841360
  46. epigenetic control of MMP-1 expression via histone H4 acetylation PMID: 20079608
  47. co-localizes with Herpes simplex virus 1 ICP0 in cell nucleus PMID: 12466471
  48. SENP1's ability to enhance AR-dependent transcription is not mediated through desumoylation of AR, but rather through its ability to deconjugate histone deacetylase 1 (HDAC1), thereby reducing its deacetylase activity. PMID: 15199155
  49. p300 is essential for SENP1 to enhance c-Jun-dependent transcription because SENP1 can desumoylate the CRD1 domain of p300, thereby releasing the cis-repression of CRD1 on p300 PMID: 15701643
  50. HIPK2 is a desumoylation target for the SUMO-specific protease SENP1 that shuttles between the cytoplasm and the nucleus. PMID: 16253240

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Subcellular Location Nucleus. Cytoplasm. Note=Shuttles between cytoplasm and nucleus.
Protein Families Peptidase C48 family
Tissue Specificity Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine.
Database Links

HGNC: 17927

OMIM: 612157

KEGG: hsa:29843

STRING: 9606.ENSP00000394791

UniGene: Hs.371957

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