Toll-free:1-888-852-8623

All categories

  • All categories
  • Flow Cytometry Antibodies
  • ELISA Kits
  • MACS Cell Isolation
  • Antibodies and Reagents
  • Apoptosis and Cell Health Detection
  • Metabolism Assays
  • Immunoassays
  • Cell Identification Kits
  • Proteins and Peptides
  • Cell Culture
Please enter the item number/product keyword!
Keyword cannot be empty !
INSERT SYMBOLS:
  • α
  • β
  • γ
  • δ
  • ε
  • ζ
  • η
  • θ
  • κ
  • μ
  • ω
  • σ
  • τ
  • λ
  • ⅩⅢ
  • ⅩⅢ
  • ⅩⅣ
  • ⅩⅤ
  • ⅩⅦ
  • ⅩⅧ
  • UP ↑

Recombinant Human Carboxypeptidase A2/CPA2 Protein (His Tag) (PKSH031569)

All Size Price Qty
50μg $ 680.00
Add to cart

For research use only.

Synonyms CPA2, Carboxypeptidase A2
Species Human
Expression Host HEK293 Cells
Sequence Met 1-Tyr 417
Accession NP_001860.2
Calculated Molecular Weight 46.0 kDa
Observed Molecular Weight 46 kDa
Tag C-His
Bio-activity Measured by its ability to cleave a colorimetric peptide substrate, N-acetyl-Phe-Thiaphe-OH (N-Ac-PSP, Peptide International's Catalog# STP-3621-PI), in the presence of 5, 5'Dithio-bis (2-nitrobenzoic acid) (DTNB), as measured using the wavelength at 405 nm and the extinction coefficient of 13, 260 M-1 cm-The specific activity is > 4, 000 pmoles/min/μg.
Purity > 90 % as determined by reducing SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method.
Storage Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping This product is provided as lyophilized powder which is shipped with ice packs.
Formulation Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.4
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution Please refer to the printed manual for detailed information.
Background Carboxypeptidase A2 ( CPA2 ) is a secreted pancreatic procarboxy -peptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties.
Other Clones

{{antibodyDetailsPage.numTotal}} Results

Other Formats

{{formatDetailsPage.numTotal}} Results

  • IF:{{item.impact}}

    Journal:{{item.journal}} ({{item.year}})

    DOI:{{item.doi}}

    Reactivity:{{item.species}}

    Sample Type:{{item.organization}}

  • Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}