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Carboxypeptidase B2 (CPB2) is a secreted enzyme that belongs to the peptidase M14 family. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen by the liver and circulates in the plasma as a plasminogen-bound zymogen. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides, such as kinins or anaphylatoxins, in the circulation regulating their activities. CPB2 also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. CPB2 exhibits carboxypeptidase activity when it is activated by proteolysis at residue Arg92 of the thrombin/thrombomodulin complex. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Pack Size | Price | Availability | Quantity |
---|---|---|---|
10 μg | $129 | 7-10 days | |
50 μg | $390 | 7-10 days | |
500 μg | $1,900 | 7-10 days | |
1 mg | $2,730 | 7-10 days |
Biological Activity | Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
Description | Carboxypeptidase B2 (CPB2) is a secreted enzyme that belongs to the peptidase M14 family. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen by the liver and circulates in the plasma as a plasminogen-bound zymogen. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides, such as kinins or anaphylatoxins, in the circulation regulating their activities. CPB2 also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. CPB2 exhibits carboxypeptidase activity when it is activated by proteolysis at residue Arg92 of the thrombin/thrombomodulin complex. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen. |
Species | Human |
Expression System | HEK293 Cells |
Tag | C-6xHis |
Accession Number | Q96IY4-1 |
Synonyms | Thrombin-Activable Fibrinolysis Inhibitor,TAFI,Plasma Carboxypeptidase B,pCPB,CPU,CPB2,Carboxypeptidase U,Carboxypeptidase B2 |
Amino Acid | Phe23-Val423 |
Construction | Phe23-Val423 |
Protein Purity | Greater than 95% as determined by reducing SDS-PAGE. Greater than 95% as determined by SEC-HPLC. |
Molecular Weight | 55-65 KDa (reducing condition) |
Endotoxin | < 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Formulation | Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, 1 mM ZnCl<sub>2</sub>, 10% Glycerol, pH8.0. |
Stability & Storage | Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
Shipping | Shipping with blue ice. |
Research Background | Carboxypeptidase B2 (CPB2) is a secreted enzyme that belongs to the peptidase M14 family. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen by the liver and circulates in the plasma as a plasminogen-bound zymogen. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides, such as kinins or anaphylatoxins, in the circulation regulating their activities. CPB2 also down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. CPB2 exhibits carboxypeptidase activity when it is activated by proteolysis at residue Arg92 of the thrombin/thrombomodulin complex. Activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen. |
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