B-type Natriuretic Peptide Human Recombinant
B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.
B-type Natriuretic Protein (27-102 a.a.) Human Recombinant
BNP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 27-102) containing 83 amino acids including a 7 a.a N-terminal His tag. The total molecular mass is 9.4kDa (calculated).
B-type Natriuretic Peptide Human
B-type Natriuretic Peptide Human Recombinant, His Tag
Natriuretic Peptide A Human Recombinant
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Natriuretic Peptide C Human Recombinant
NT-Pro-B-type Natriuretic Protein Canine Recombinant
NT-proBNP Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-85 a.a) containing 101 a.a and having a molecular mass of 10,545 Dalton. NT-proBNP is fused with a 16 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
NT-Pro-B-type Natriuretic Protein Human Recombinant
NT-Pro-B-type Natriuretic Protein Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acid and having a molecular mass of approximately 8.5kDa.
NT-proBNP is purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile Filtered White lyophilized (freeze-dried) powder.
Pro B-type Natriuretic Protein Human Recombinant
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.
Escherichia Coli.
Sterile Filtered colorless liquid formulation.
B-type Natriuretic Peptide (BNP), also known as brain natriuretic peptide, is a member of the natriuretic peptide family of protein hormones. It is primarily produced in the heart’s ventricles in response to volume expansion and pressure overload . BNP is classified alongside other natriuretic peptides such as atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP) .
Key Biological Properties: BNP is a 32-amino acid polypeptide with a disulfide bond between two cysteine residues, essential for its biological activity . It is synthesized as a preprohormone, cleaved to proBNP, and then further processed to BNP and NT-proBNP .
Expression Patterns and Tissue Distribution: BNP is predominantly expressed in the cardiac ventricles, but it can also be found in the brain, kidneys, and other tissues . Its expression is upregulated in response to cardiac stress and heart failure .
Primary Biological Functions: BNP plays a crucial role in cardiovascular homeostasis by promoting natriuresis (excretion of sodium in urine), diuresis (increased urine production), and vasodilation (widening of blood vessels) . It helps reduce blood volume and pressure, thereby decreasing the workload on the heart .
Role in Immune Responses and Pathogen Recognition: While BNP’s primary functions are cardiovascular, it also exhibits anti-inflammatory properties and can modulate immune responses .
Mechanisms with Other Molecules and Cells: BNP exerts its effects by binding to natriuretic peptide receptors (NPRs), particularly NPR-A, which activates guanylyl cyclase and increases cyclic GMP (cGMP) levels . This signaling cascade leads to vasodilation, natriuresis, and diuresis .
Binding Partners and Downstream Signaling Cascades: BNP interacts with NPR-A and NPR-C receptors. NPR-A mediates its primary effects through cGMP, while NPR-C is involved in the clearance of BNP from circulation .
Regulatory Mechanisms Controlling Expression and Activity: BNP expression is regulated at the transcriptional level by factors such as myocardial stretch and neurohormonal activation . Post-translational modifications, including glycosylation and proteolytic cleavage, also play a role in its activity .
Transcriptional Regulation and Post-Translational Modifications: Transcription factors like NFAT and GATA4 are involved in the upregulation of BNP gene expression in response to cardiac stress . Post-translational modifications ensure proper folding and stability of the peptide .
Biomedical Research: BNP is extensively studied as a biomarker for heart failure and other cardiovascular diseases . Its levels correlate with the severity of heart failure and can guide treatment decisions .
Diagnostic Tools: BNP and NT-proBNP assays are widely used in clinical practice to diagnose heart failure, assess its severity, and monitor treatment efficacy .
Therapeutic Strategies: BNP analogs and recombinant BNP (nesiritide) are used therapeutically to manage acute decompensated heart failure by promoting vasodilation and diuresis .
Role Throughout the Life Cycle: BNP levels vary throughout life, increasing with age and in response to cardiac stress . Elevated BNP levels are associated with aging-related cardiovascular diseases, such as heart failure and hypertension . Monitoring BNP levels can provide insights into cardiovascular health from development through aging and disease .