CPB2 Antibody (Center E134) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q96IY4 |
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Clone Names | 80410133 |
Gene ID | 1361 |
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Other Names | Carboxypeptidase B2, Carboxypeptidase U, CPU, Plasma carboxypeptidase B, pCPB, Thrombin-activable fibrinolysis inhibitor, TAFI, CPB2 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6541c was selected from the Center region of human CPB2. 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 | CPB2 |
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Function | Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. |
Cellular Location | Secreted. |
Tissue Location | Plasma; synthesized in the liver. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). CPB2 is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for its gene and its promoter region.
References
Valnickova,Z., J. Biol. Chem. 271 (22), 12937-12943 (1996)
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