Carboxypeptidase A2 cDNA ORF Clone in Cloning Vector, Cynomolgus

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Carboxypeptidase A2 cDNA ORF Clone in Cloning Vector, Cynomolgus: General Information

Gene
Species
Cynomolgus
NCBI Ref Seq
RefSeq ORF Size
1266 bp
Sequence Description
Identical with the Gene Bank Ref. ID sequence except for the point mutations: 140A/T(E47V), 571G/A(A191T); 12G/A not causing the amino acid variation. Please check the sequence information before order.
Description
Full length Clone DNA of Cynomolgus carboxypeptidase A2 (pancreatic).
Plasmid
Vector
Sequencing Primers
M13-47 and RV-M
Quality Control
The plasmid is confirmed by full-length sequencing.
Screening
Antibiotic in E.coli
Ampicillin
Storage & Shipping
Shipping
Each tube contains lyophilized plasmid.
Storage
The lyophilized plasmid can be stored at ambient temperature for three months.

Carboxypeptidase A2 cDNA ORF Neucleotide Sequence and Amino Acid Sequence Information

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

Carboxypeptidase A2 cDNA ORF Clone in Cloning Vector, Cynomolgus: Validated Images

Carboxypeptidase A2 Background Information

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.
Full Name
carboxypeptidase A2
References
  • Catasus, L. et al., 1995. J. Biol. Chem. 270: 6651-6657.
  • Aloy, P. et al., 1998, Biol. Chem. 379: 149-155.
  • Laethem, RM. et al., 1996, Arch. Biochem. Biophys.332: 8-18.
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