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CPN1 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P15169 |
|---|---|
| Clone Names | 80410141 |
| Gene ID | 1369 |
|---|---|
| Other Names | Carboxypeptidase N catalytic chain, CPN, Anaphylatoxin inactivator, Arginine carboxypeptidase, Carboxypeptidase N polypeptide 1, Carboxypeptidase N small subunit, Kininase-1, Lysine carboxypeptidase, Plasma carboxypeptidase B, Serum carboxypeptidase N, SCPN, CPN1, ACBP |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7337a was selected from the N-term region of human CPN1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | CPN1 |
|---|---|
| Synonyms | ACBP |
| Function | Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. |
| Cellular Location | Secreted, extracellular space. |
| Tissue Location | Synthesized in the liver and secreted in plasma. |
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Provided below are standard protocols that you may find useful for product applications.
Background
CPN1 is a plasma metallo-protease that cleaves basic amino acids from the C terminal of peptides and proteins. The protein is important in the regulation of peptides like kinins and anaphylatoxins, and has also been known as kininase-1 and anaphylatoxin inactivator. This protein is a tetramer comprised of two identical regulatory subunits and two identical catalytic subunits.
References
Davis,D.A., Singer,K.E. Blood 105 (12), 4561-4568 (2005)Riley,D.A., Tan,F. Genomics 50 (1), 105-108 (1998)Hendriks,D., Vingron,M. Biol. Chem. Hoppe-Seyler 374 (9), 843-849 (1993)
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