Rabbit polyclonal to SENP2
Synthetic peptide containing a sequence corresponding to a region within N terminal amino acids 1 and 32 of Human SENP2 (NP_067640).
A431, H1299, HepG2, Raji cell lysates. 293T and Molt-4 whole cell lysates. A431 cells and Cal27 xenograft.
Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 10% Glycerol, 0.1M Tris, 0.1M Glycine, pH 7
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Immunogen affinity purified
Abpromise guarantee covers the use of
in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/500 - 1/3000. Predicted molecular weight: 68 kDa.
1/100 - 1/500.
1/100 - 1/200.
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. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway.
Belongs to the peptidase C48 family.
The N-terminus is necessary and sufficient for nuclear envelope targeting.
Polyubiquitinated; which leads to proteasomal degradation.
Nucleus > nuclear pore complex. Nucleus membrane. Cytoplasm. Shuttles between cytoplasm and nucleus.
Information by UniProt
Western blot - Anti-SENP2 antibody (ab96865)
All lanes : Anti-SENP2 antibody (ab96865) at 1/1000 dilution Lane 1 : 293T whole cell lysate Lane 2 : MOLT-4 whole cell lysate Lysates/proteins at 30 µg per lane. Predicted band size: 68 kDa 7.5% SDS PAGE
Immunocytochemistry/ Immunofluorescence - Anti-SENP2 antibody (ab96865)
Immunofluorescence analysis of paraformaldehyde-fixed A431, using SENP2 antibody (ab96865) at 1/200 dilution. Lower image merged with DNA probe.
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-SENP2 antibody (ab96865)
Immunohistochemical analysis of paraffin-embedded Cal27 xenograft, using SENP2 antibody (ab96865) at 1/500 dilution.
has not yet been referenced specifically in any publications.
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