Product List

BNP

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. 

Shipped with Ice Packs
Cat. No.
BT19007
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BNP (27-102) Human

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). 

Shipped with Ice Packs
Cat. No.
BT19099
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

BNP Human

B-type Natriuretic Peptide Human

B-type Natriuretic Peptide Human is a polypeptide chain containing 32 amino acids and having a molecular mass of 3464 Dalton. The molecular formula is:C143H244N50O42S4.
Shipped with Ice Packs
Cat. No.
BT19185
Source
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BNP Human, His

B-type Natriuretic Peptide Human Recombinant, His Tag

BNP Recombinant Human fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids (27-134 a.a) and having a molecular mass of 14 kDa.                   
BNP is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19315
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

NPPA Human

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). 

Shipped with Ice Packs
Cat. No.
BT19388
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

NPPC Human

Natriuretic Peptide C Human Recombinant

NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.
NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19462
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

NT-proBNP Canine

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.

Shipped with Ice Packs
Cat. No.
BT19544
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

NT-proBNP Human

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.

Shipped with Ice Packs
Cat. No.
BT19647
Source

Escherichia Coli.

Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

proBNP Human

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.

Shipped with Ice Packs
Cat. No.
BT19713
Source

Escherichia Coli.

Appearance

Sterile Filtered colorless liquid formulation.

Introduction

Definition and Classification

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) .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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

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 .

Applications

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 in the Life Cycle

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 .

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