Carboxypeptidase E cDNA ORF Clone, Mouse, N-HA tag General Information
Full length Clone DNA of Mouse carboxypeptidase E with N terminal HA tag.
Enhanced CMV promoter
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
The plasmid is confirmed by full-length sequencing.
Antibiotic in E.coli
Antibiotic in Mammalian cell
Stable or Transient mammalian expression
Storage & Shipping
Each tube contains lyophilized plasmid.
The lyophilized plasmid can be stored at ambient temperature for three months.
**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 E cDNA ORF Clone, Mouse, N-HA tag Alternative Names
CPH cDNA ORF Clone, Mouse;Cph-1 cDNA ORF Clone, Mouse;Cph1 cDNA ORF Clone, Mouse;fat cDNA ORF Clone, Mouse;R74677 cDNA ORF Clone, Mouse
Carboxypeptidase E Background Information
Carboxypeptidase E (CPE), also known as Carboxypeptidase H, is a peripheral membrane protein and a zinc metallocarboxypeptidase, and the conversion of proCPE into CPE occurs primarily in secretory vesicles. The active form of CPE cleaves C-terminal amino acid residues of the peptide, and is thus involved in the biosynthesis of peptide hormones and neurotransmitters including insulin, enkephalin, etc. The enzymatic activity is enhanced by millimolar concentrations of Co2+. It has also been proposed that membrane-associated carboxypeptidase E acts as a sorting receptor for targeting regulated secretory proteins which are mostly prohormones and neuropeptides in the trans-Golgi network of the pituitary and in secretory granules into the secretory pathway.Its interaction with glycosphingolipid-cholesterol rafts at the TGN facilitates the targeting. Mutations in this gene are implicated in type I I diabetes due to impaired glucose clearance and insulin resistance.
Manser, E. et al., 1990, Biochem. J. 267: 517-525. Cool, D.R. et al., 1997, Cell. 88: 73-83. Song, L. and Fricker, L. 1995, J. Neurochem. 65: 444-453. Dhanvantari,S. et al., 2000, J. Biol. Chem. 275: 29887-29893. Jeffrey, K.D. et al., 2008, Proc. Natl. Acad. Sci. U.S.A. 105: 8452-8457