Recombinant Saccharomyces cerevisiae Ubiquitin-like-specific protease 1(ULP1),partial CSB-EP311619SVG
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
ULP1; YPL020C; LPB11C; Ubiquitin-like-specific protease 1; EC 3.4.22.68
Species: (Organism)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Gene Names:
ULP1
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
LVPRGSHMASLVPELNEKDDDQVQKALASRENTQLMNRDNIEITVRDFKTLAPRRWLNDTIIEFFMKYIEKSTPNTVAFNSFFYTNLSERGYQGVRRWMKRKKTQIDKLDKIFTPINLNQSHWALGIIDLKKKTIGYVDSLSNGPNAMSFAILTDLQKYVMEESKHTIGEDFDLIHLDCPQQPNGYDCGIYVCMNTLYGSADAPLDFDYKDAIRMRRFIAHLILTDALK
Expression Region:
403-621aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Partial
Pathway:
Mol. Weight:
27.9 kDa
Purity:
Greater than 90% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Others
Function:
Protease that catalyzes two essential functions in the SUMO pathway
Involvement in disease:
Relevance:
Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle.
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.
Protein Families:
Peptidase C48 family
Reference:
"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008)
