Recombinant Mouse Carboxypeptidase B2/CPB2 Protein (His Tag)
Size: 100μg
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Exp date: 12 months
Category ID_II: Recombinant Proteins
Category ID_III: Others
Abbreviation:
Target Synonym: 1110032P04Rik;4930405E17Rik;AI255929;CPR;Cpu;TAFI
Research Areas:
Conjugation:
Target Species: Mouse
Expression Host: HEK293 Cells
Application:
Fusion tag: C-His
UNIProt ID: Q9JHH6
Accession: Q9JHH6
Background: Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. 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 thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin / thrombomodulin complex. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. CPB2 exhibits carboxypeptidase activity and activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Concentration:
Activity: Not validated for activity
Sequence: Met 1-Thr 422
Purity: > 97 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 48.0 kDa
ObservedMW: 60 kDa
Product Information
Product Information
Shipping & Returns
Shipping & Returns
Recombinant Mouse Carboxypeptidase B2/CPB2 Protein (His Tag)
Recombinant Mouse Carboxypeptidase B2/CPB2 Protein (His Tag)
Size: 100μg
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Exp date: 12 months
Category ID_II: Recombinant Proteins
Category ID_III: Others
Abbreviation:
Target Synonym: 1110032P04Rik;4930405E17Rik;AI255929;CPR;Cpu;TAFI
Research Areas:
Conjugation:
Target Species: Mouse
Expression Host: HEK293 Cells
Application:
Fusion tag: C-His
UNIProt ID: Q9JHH6
Accession: Q9JHH6
Background: Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. 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 thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin / thrombomodulin complex. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. CPB2 exhibits carboxypeptidase activity and activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Concentration:
Activity: Not validated for activity
Sequence: Met 1-Thr 422
Purity: > 97 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 48.0 kDa
ObservedMW: 60 kDa
Product Information
Product Information
Shipping & Returns
Shipping & Returns
Description
Size: 100μg
Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Exp date: 12 months
Category ID_II: Recombinant Proteins
Category ID_III: Others
Abbreviation:
Target Synonym: 1110032P04Rik;4930405E17Rik;AI255929;CPR;Cpu;TAFI
Research Areas:
Conjugation:
Target Species: Mouse
Expression Host: HEK293 Cells
Application:
Fusion tag: C-His
UNIProt ID: Q9JHH6
Accession: Q9JHH6
Background: Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. 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 thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin / thrombomodulin complex. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. CPB2 exhibits carboxypeptidase activity and activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Concentration:
Activity: Not validated for activity
Sequence: Met 1-Thr 422
Purity: > 97 % as determined by reducing SDS-PAGE.
Formulation: Lyophilized from sterile PBS, pH 7.4
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.
Reconstitution: Please refer to the printed manual for detailed information.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Calculated MW: 48.0 kDa
ObservedMW: 60 kDa
