Carboxypeptidase B2 Recombinant Protein | CPB2 recombinant protein

Carboxypeptidase B2 Protein, Rat, Recombinant (His Tag)

Cat. Num. AAA8123501

• Purity: >95% as determined by SDS-PAGE
• Synonyms: Carboxypeptidase B2; Carboxypeptidase B2 Protein; Rat; Recombinant (His Tag); Rat Carboxypeptidase B2/CPB2 Protein (His Tag); carboxypeptidase B2 (plasma); CPB2 recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Ser422

• Species: Rat
• Endotoxin: <1.0EU per ug protein as determined by the LAL method.
• Predicted N Terminal: Phe 22
• Tag: C-His
• Protein Construction: A DNA sequence encoding the rat Cpb2 (NP_446069.1)(Met1-Ser422) was expressed with a polyhistidine tag at the C-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for CPB2 recombinant protein

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.

References

Eaton DL. et al.,1991, J Biol Chem. 266 (32): 21833-8. Boffa MB. et al.,1999, Biochemistry. 38 (20): 6547-58. Liu T. et al., 2005, J. Proteome Res. 4: 2070-80. Valnickova Z. et al., 2006, Biochemistry. 45: 1525-35. Chen R. et al., 2009, J. Proteome Res. 8: 651-61.

NCBI and Uniprot Product Information

• NCBI GI #: 16758414
• NCBI GeneID: 113936
• NCBI Accession #: NP_446069.1
• NCBI GenBank Nucleotide #: NM_053617.2
• UniProt Accession #: Q9EQV9; Q3B7V3; Q5BKB8
• Molecular Weight: 48,827 Da
• NCBI Official Full Name: carboxypeptidase B2
• NCBI Official Synonym Full Names: carboxypeptidase B2
• NCBI Official Symbol: Cpb2
• NCBI Protein Information: carboxypeptidase B2
• UniProt Protein Name: Carboxypeptidase B2
• Protein Family: Carboxypeptidase
• UniProt Gene Name: Cpb2
• UniProt Synonym Gene Names: CPR; CPU; TAFI

NCBI Description

a thrombin-activatable fibrinolysis inhibitor [RGD, Feb 2006]

Uniprot Description

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.