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CPB2 Protein, Human, Recombinant (His)

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CPB2 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00649

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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Pack Size	Price	Availability
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

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Biological Description

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	CPB2,CPU,TAFI,pCPB,Carboxypeptidase B2,Plasma Carboxypeptidase B,Thrombin-Activable Fibrinolysis Inhibitor,Carboxypeptidase U
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	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry 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.