Recombinant Human Sentrin-specific protease 2 (SENP2)

Code CSB-YP888026HU
MSDS
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Source Yeast
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Code CSB-EP888026HU
MSDS
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Source E.coli
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Code CSB-EP888026HU-B
MSDS
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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-BP888026HU
MSDS
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Source Baculovirus
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Code CSB-MP888026HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Axam2; DKFZp762A2316; KIAA1331; Senp2; SENP2_HUMAN; Sentrin specific protease 2; Sentrin-specific protease 2; Sentrin/SUMO specific protease SENP2; Sentrin/SUMO-specific protease SENP2; SMT3 specific isopeptidase 2; SMT3-specific isopeptidase 2; Smt3ip2; SUMO1/sentrin/SMT3 specific peptidase 2
Species
Homo sapiens (Human)
Expression Region
1-589
Target Protein Sequence
MYRWLVRILG TIFRFCDRSV PPARALLKRR RSDSTLFSTV DTDEIPAKRP RLDCFIHQVK NSLYNAASLF GFPFQLTTKP MVTSACNGTR NVAPSGEVFS NSSSCELTGS GSWNNMLKLG NKSPNGISDY PKIRVTVTRD QPRRVLPSFG FTLNSEGCNR RPGGRRHSKG NPESSLMWKP QEQAVTEMIS EESGKGLRRP HCTVEEGVQK EEREKYRKLL ERLKESGHGN SVCPVTSNYH SSQRSQMDTL KTKGWGEEQN HGVKTTQFVP KQYRLVETRG PLCSLRSEKR CSKGKITDTE TMVGIRFENE SRRGYQLEPD LSEEVSARLR LGSGSNGLLR RKVSIIETKE KNCSGKERDR RTDDLLELTE DMEKEISNAL GHGPQDEILS SAFKLRITRG DIQTLKNYHW LNDEVINFYM NLLVERNKKQ GYPALHVFST FFYPKLKSGG YQAVKRWTKG VNLFEQEIIL VPIHRKVHWS LVVIDLRKKC LKYLDSMGQK GHRICEILLQ YLQDESKTKR NSDLNLLEWT HHSMKPHEIP QQLNGSDCGM FTCKYADYIS RDKPITFTQH QMPLFRKKMV WEILHQQLL
Protein Length
full length protein
Tag Info
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.
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.
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
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. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway. Deconjugates SUMO2 from MTA1. Plays a dynamic role in adipogenesis by desumoylating and promoting the stabilization of CEBPB.
Gene References into Functions
  1. research achievements of SENP2 are reviewed in order to understand its related functions and the underlying molecular mechanisms and provide a clue for future research on SENP2 PMID: 29908207
  2. Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO conjugation via the inhibition of SUMO-specific protease (SENP)2. PMID: 29146736
  3. Data demonstrate that downregulation of SENP2 is correlated with poor prognosis in bladder cancer; SENP2 inhibits TGF-beta signaling and TGF-beta-induced EMT of bladder cancer cell; and that its overexpression contributes to suppress bladder cancer cell invasion and metastasis through deSUMOylation of TGF-betaRI. PMID: 28574613
  4. The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence. PMID: 27178176
  5. SENP2 inhibits MMP13 expression in BC cells through de-SUMOylation of TBL1/TBLR1, which inhibits nuclear translocation of beta-catenin. PMID: 26369384
  6. miR-181b targets SENP2 and positively regulated NF-kappaB activity. NF-kappaB activation by DNA damage in GBM cells confers resistance to radiation-induced death. PMID: 25633526
  7. data identify SENP2 as an important regulator of fatty acid metabolism in skeletal muscle PMID: 25784542
  8. SENP2 regulates the transcriptional function of MEF2A via direct de-SUMOylation. PMID: 25483061
  9. p90RSK-mediated SENP2-T368 phosphorylation is a master switch in disturbed-flow-induced signaling. PMID: 25689261
  10. ESR1 repression by SENP2 is independent of its SUMO protease activity. PMID: 24422630
  11. Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted. PMID: 24196834
  12. Chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis; SENP1 and SENP2 are important mediators of this control. PMID: 24048451
  13. The SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance. PMID: 22688647
  14. SENP2 inhibited bladder cancer cells migration and invasion by regulating the expression of MMP13. PMID: 24008762
  15. SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation. PMID: 23224591
  16. SENP2 represses glycolysis and shifts glucose metabolic strategy PMID: 23691130
  17. SENP2 regulates hepatocellular carcinoma cell growth by modulating the stability of beta-catenin. PMID: 23098437
  18. cardiac overexpression of SENP2 in the mice with Nkx2.5 haploinsufficiency promoted embryonic lethality and severity of congenital heart diseases (CHDs). PMID: 22155005
  19. Data suggest that SENP2 regulates antiviral innate immunity by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation, and provide an example of cross-talk between the ubiquitin and SUMO pathways in innate immunity. PMID: 22028379
  20. SENP2 null cells display biphasic NEMO SUMOylation and activation of IKK and NF-kappaB PMID: 21777808
  21. a mechanism underlying the SENP2-mediated regulation of Mdm2 that is critical for genome integrity in p53-dependent stress responses. PMID: 21183956
  22. Results demonstrate that SENP1 is the most efficient SUMO protease acting on Elk-1, and that SENP3 has little effect on Elk-1. SENP2 has an intermediate effect, but its ability to activate Elk-1 is independent from its SUMO-deconjugating activity. PMID: 20337593
  23. association with the pore plays an important negative role in the regulation of SENP2 PMID: 11896061
  24. Restricting SENP2 in the nucleus by mutations in the NES impairs its polyubiquitination, whereas a cytoplasm-localized SENP2 made by introducing mutations in the NLS can be efficiently polyubiquitinated. PMID: 16738331
  25. Mutational analysis and biochemistry provide a mechanism for SENP2 substrate preferences that explains why SENP2 catalyzes SUMO deconjugation more efficiently than processing PMID: 17099700

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Subcellular Location
Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm.
Protein Families
Peptidase C48 family
Database Links

HGNC: 23116

OMIM: 608261

KEGG: hsa:59343

STRING: 9606.ENSP00000296257

UniGene: Hs.401388

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