CPN1
CPN1 (carboxypeptidase N subunit 1) is the catalytic chain of carboxypeptidase N, a secreted plasma metallo-protease that removes C-terminal basic residues from peptides and proteins. It helps protect the body from potent vasoactive and inflammatory peptides such as kinins and anaphylatoxins. Browse Assay Genie's current range of CPN1 research reagents below, or read on for the biology behind the target.
Carboxypeptidase N is a plasma metallo-protease that cleaves basic amino acids from the C terminus of peptides and proteins. Its substrates include peptides that end in C-terminal arginine or lysine, such as kinins and anaphylatoxins, which are released into the circulation. By trimming these potent vasoactive and inflammatory peptides, the enzyme protects the body from their effects. For this reason it has also been known as kininase-1 and anaphylatoxin inactivator.
The active enzyme is a tetramer made up of two identical regulatory subunits and two identical catalytic subunits. The CPN1 gene encodes the catalytic subunit, and the CPN1 protein is found as a secreted protein in the extracellular space. The regulatory subunit is encoded by a separate gene, CPN2. CPN1 belongs to the peptidase M14 family and is classified by HGNC within the M14 carboxypeptidases gene group. Mouse and rat each have an ortholog named Cpn1.
The gene was previously named carboxypeptidase N, polypeptide 1, 50kD. Mutations in CPN1 can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency, which links the enzyme to the control of kinin and anaphylatoxin activity. This makes carboxypeptidase N a useful subject for studies of peptide regulation in plasma.
CPN1 acts as kininase-1, removing C-terminal basic residues from kinins and so limiting the activity of these vasoactive peptides in the circulation.
As an anaphylatoxin inactivator, CPN1 helps protect the body from inflammatory peptides carrying C-terminal Arg or Lys.
Mutations in CPN1 can be associated with angioedema or chronic urticaria caused by carboxypeptidase N deficiency.
CPN1 is the catalytic subunit of a tetrameric plasma metallo-protease and a member of the M14 carboxypeptidase family.
CPN1 is the catalytic subunit of carboxypeptidase N, a plasma metallo-protease. It cleaves basic amino acids from the C terminus of peptides and proteins, protecting the body from vasoactive and inflammatory peptides, such as kinins and anaphylatoxins, that are released into the circulation.
The enzyme is called carboxypeptidase N catalytic chain in UniProt, and carboxypeptidase N has also been known as kininase-1 and anaphylatoxin inactivator. The gene was previously named carboxypeptidase N, polypeptide 1, 50kD. It is the catalytic subunit of a tetramer with two regulatory subunits.
Mouse and rat both have an ortholog named Cpn1; check the datasheet of any product for its validated reactivity. In humans, CPN1 mutations can be associated with angioedema or chronic urticaria resulting from carboxypeptidase N deficiency.
The regulatory partner of CPN1 and other related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P15169; product specifications from Assay Genie datasheets.