What is Human carboxypeptidase N and how it works
What is Human carboxypeptidase N and how it works
— An extracellular glycoprotein synthesized in the liver and secreted into the blood.
— Controls the activity of vasoactive peptide hormones, growth factors and cytokines by specifically removing C-terminal basic residues such as Arg or Lys.
— A member of the CPN/E subfamily of “regulatory” metallo-carboxypeptidases.
— Circulates in blood plasma as a hetero-tetramer consisting of two 83 kDa (CPN2) domains each flanked by a 48 to 55 kDa catalytic (CPN1) domain.
The 280 kDa form of CPN is a dimer of heterodimers, with each heterodimer containing one catalytic subunit and one 83 kDa subunit.
The 83 kDa protein is a non-catalytic regulatory subunit whereas the 55 kDa and 48 kDa proteins represent the native or proteolytically cleaved forms of the active subunit.
Figure 1.Molecular model of the 83 kDa subunit of CPN. A three-dimensional homology model of the 83 kDa subunit.
Figure 2.Stereo image of the structure of the catalytic subunit of human CPN. The ribbon representation shows the catalytic domain on top and the cylindrical TT domain at the bottom.
Reference:
- Crystal Structure of the Human Carboxypeptidase N (Kininase I) Catalytic Domain
- Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator
Echo Biosystems have developed a series of high-quality Human carboxypeptidase N protein antibody to meet your research needs.
| CPN1 Polyclonal Antibody | CPN1 from Yeast | CPN1 from Baculovirus |
| CPN1 from E.coli | CPN1 Mammalian cell | |
| CPN2 from Yeast | CPN12 from Baculovirus | CPN2 from E.coli |
| CPN2 from Mammalian cell |