Escherichia Coli.
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide
Sterile Filtered colorless liquid formulation.
Greater than 90.0% as determined by SDS-PAGE.
Recombinant Human Pro B-type Natriuretic Protein produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa1-108), fused to His-tag and having a molecular weight of ~13kDa.
The proBNP is purified by proprietary chromatographic techniques.
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide
Escherichia Coli.
Pro B-type Natriuretic Protein (proBNP) is a precursor molecule that plays a crucial role in cardiovascular homeostasis. It is a cardiac hormone with various biological actions, including natriuresis (excretion of sodium in the urine), diuresis (increased urine production), vasorelaxation (relaxation of blood vessels), and inhibition of renin and aldosterone secretion . The recombinant form of this protein, produced using bioengineering techniques, offers significant potential in the field of cardiovascular medicine.
Recombinant human proBNP is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain consisting of 108 amino acids. This recombinant protein is fused to a His-tag and has a molecular weight of approximately 13 kDa . The production process involves proprietary chromatographic techniques to purify the protein, ensuring a high level of purity (greater than 90% as determined by SDS-PAGE) .
ProBNP is processed into its active form, B-type Natriuretic Peptide (BNP), and its N-terminal fragment (NT-proBNP) through enzyme-mediated cleavage. BNP and NT-proBNP are well-established biomarkers for heart failure and are routinely used by clinicians for the exclusion of heart failure and risk assessment in patients with acute coronary syndromes . The active BNP hormone, comprising 32 amino acid residues, along with the physiologically inactive NT-proBNP, plays a key role in maintaining cardiovascular homeostasis by increasing sodium excretion, reducing cardiac load, and lowering blood pressure .
The processing of proBNP involves specific enzymes, such as furin and corin, which cleave the precursor molecule into distinct BNP forms. Furin-mediated cleavage results in BNP 1-32, while corin-mediated cleavage produces BNP 4-32 . These enzymes play a critical role in the regulation of BNP physiology and the maintenance of cardiovascular function .
The recombinant form of proBNP has been extensively studied for its potential therapeutic applications in cardiovascular diseases. In vitro studies have shown that proBNP interacts with cardiomyocytes and the cyclic guanosine monophosphate (cGMP) signaling pathway, which is essential for cardiovascular homeostasis . In vivo studies using animal models have demonstrated the potential effects of proBNP in managing heart failure and improving overall heart function .