Recombinant Elizabethkingia meningoseptica Proline iminopeptidase(fpaP) CSB-EP516921FEW
Specifications
| 20ug / 200ug price = 20ug |
Alternative Name(s):
Prolyl aminopeptidase (PAP)
Species: (Organism)
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Gene Names:
fpaP
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
MIPITTPVGNFKVWTKRFGTNPKIKVLLLHGGPAMTHEYMECFETFFQREGFEFYEYDQLGSYYSDQPTDEKLWNIDRFVDEVEQVRKAIHADKENFYVLGNSWGGILAMEYALKYQQNLKGLIVANMMASAPEYVKYAEVLSKQMKPEVLAEVRAIEAKKDYANPRYTELLFPNYYAQHICRLKEWPDALNRSLKHVNSTVYTLMQGPSELGMSSDARLAKWDIKNRLHEIATPTLMIGARYDTMDPKAMEEQSKLVQKGRYLYCPNGSHLAMWDDQKVFMDGVIKFIKDVDTKSFN
Expression Region:
1-298aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
41.6 kDa
Purity:
Greater than 85% 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:
Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA.
Involvement in disease:
Relevance:
Releases the N-terminal proline from various substrates. Cleaves specifically Pro-betaNA and small peptides containing proline at the amino terminal. No activity against hydroxyproline-betaNA.
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 S33 family
Reference:
"Prolyl aminopeptidase gene from Flavobacterium meningosepticum: cloning, purification of the expressed enzyme, and analysis of its sequence." Kitazono A., Kabashima T., Huang H.S., Ito K., Yoshimoto T. Arch. Biochem. Biophys. 336:35-41(1996)
