Carboxypeptidase B2/CPB2 Protein, Rat (HEK293, His)

Carboxypeptidase B2 (CPB2) protein acts as an enzyme that cleaves C-terminal arginine or lysine residues from biologically active peptides, including kinins or anaphylatoxins circulating in the blood, thereby regulating their activity. Furthermore, CPB2 plays a key role in downregulating fibrinolysis by removing C-terminal lysine residues from fibrin that has been partially degraded by plasmin. Carboxypeptidase B2/CPB2 Protein, Rat (HEK293, His) is the recombinant rat-derived Carboxypeptidase B2/CPB2 protein, expressed by HEK293 , with C-His labeled tag. The total length of Carboxypeptidase B2/CPB2 Protein, Rat (HEK293, His) is 422 a.a., with molecular weight of ~48 kDa.

CaCarboxypeptidase B2 (CPB2) plays a critical role in physiological regulation, particularly within the circulatory system. The enzyme exhibits specificity in cleaving C-terminal arginine or lysine residues from biologically active peptides, including kinins and anaphylatoxins, thereby finely tuning their activities and downstream signaling in the circulation. Additionally, CPB2 is instrumental in the down-regulation of fibrinolysis by selectively removing C-terminal lysine residues from fibrin that has undergone partial degradation by plasmin. This dual functionality underscores CPB2's pivotal role in maintaining the balance of peptide activities and coagulation processes, emphasizing its significance in orchestrating intricate regulatory mechanisms within the physiological context.

Rat

HEK293

C-His

Q9EQV9 (M1-S422)

113936  [NCBI]

Approximately 48 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.