Recombinant Human Carboxypeptidase B2/CPB2 Protein (His Tag) (PKSH032172)
For research use only.
Synonyms | CPB2, CPU, Carboxypeptidase B2, Carboxypeptidase U, Plasma Carboxypeptidase B, TAFI, Thrombin-Activable Fibrinolysis Inhibitor, pCPB |
Species | Human |
Expression Host | HEK293 Cells |
Sequence | Phe23-Val423 |
Accession | NP_001863.3 |
Calculated Molecular Weight | 47.0 kDa |
Observed Molecular Weight | 55-65 kDa |
Tag | C-His |
Bio-activity | Not validated for activity |
Purity | > 95 % as determined by reducing SDS-PAGE. |
Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
Formulation | Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM ZnCl2, 10% Glycerol, pH8.0. |
Reconstitution | Not Applicable |
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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