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>   首页   >   产品   >   一抗   >   细胞生物学   >   SENP1 Antibody (C-term)   

SENP1 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SENP1 Antibody (C-term) AP1231a
    Anti-SENP1 Antibody (C-term) at 1:1000 dilution + PANC-1 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 73 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q9P0U3
Other Accession P59110
Reactivity Human
Predicted Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 73481 Da
Antigen Region 560-590 aa
Additional Information
Gene ID 29843
Other Names Sentrin-specific protease 1, Sentrin/SUMO-specific protease SENP1, SENP1
Target/Specificity This SENP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 560-590 amino acids from the C-terminal region of human SENP1.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsSENP1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SENP1
Function Protease that catalyzes two essential functions in the SUMO pathway (PubMed:10652325, PubMed:15199155, PubMed:15487983, PubMed:16253240, PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). 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 (PubMed:15487983). 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 (PubMed:15199155, PubMed:16253240, PubMed:21829689, PubMed:21965678, PubMed:23160374, PubMed:24943844, PubMed:25406032, PubMed:29506078, PubMed:34048572, PubMed:37257451). Deconjugates SUMO1 from HIPK2 (PubMed:16253240). Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity (PubMed:15199155, PubMed:21829689). Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity (PubMed:23160374). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Inhibits N(6)-methyladenosine (m6A) RNA methylation by mediating SUMO1 deconjugation from METTL3 and ALKBH5: METTL3 inhibits the m6A RNA methyltransferase activity, while ALKBH5 desumoylation promotes m6A demethylation (PubMed:29506078, PubMed:34048572, PubMed:37257451). Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032). Deconjugates SUMO1 from GPS2 (PubMed:24943844).
Cellular Location Nucleus. Cytoplasm Note=Shuttles between cytoplasm and nucleus
Tissue Location Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

SENP1 is a protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. SENP deconjugates SUMO1 from HIPK2 and from HDAC1, which decreases the transcriptional repression activity of the latter.

REFERENCES

Gong, L., et al., J. Biol. Chem. 275(5):3355-3359 (2000).
Bailey, D., et al., J. Gen. Virol. 83 (Pt 12), 2951-2964 (2002).

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