BNP

B-type Natriuretic Peptide Human Recombinant

Recombinant Human B-type Natriuretic Peptide, produced in E. coli, is a single-chain polypeptide consisting of 32 amino acids. It is non-glycosylated and has a molecular weight of 3,500 Daltons. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19007
Source
Escherichia Coli.
Appearance
White, lyophilized powder, sterile-filtered.

BNP (27-102) Human

B-type Natriuretic Protein (27-102 a.a.) Human Recombinant

Recombinant Human BNP, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 83 amino acids (a.a 27-102). It includes a 7 a.a N-terminal His tag and has a molecular weight of 9.4kDa (calculated).

Shipped with Ice Packs
Cat. No.
BT19099
Source
Escherichia Coli.
Appearance
The product appears as a white powder that has been filtered and lyophilized (freeze-dried).

BNP Human

B-type Natriuretic Peptide Human

Human B-type natriuretic peptide is a polypeptide composed of 32 amino acids, with a molecular weight of 3464 Daltons. Its molecular formula is C143H244N50O42S4.
Shipped with Ice Packs
Cat. No.
BT19185
Appearance
Sterile filtered white lyophilized powder.

BNP Human, His

B-type Natriuretic Peptide Human Recombinant, His Tag

Recombinant Human BNP, with a 20 amino acid His tag attached to its N-terminus, is produced in E. coli bacteria. This results in a single, non-glycosylated polypeptide chain comprising 129 amino acids (specifically, amino acids 27 to 134). It has a molecular weight of 14 kDa. The purification of BNP is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19315
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

NPPA Human

Natriuretic Peptide A Human Recombinant

Recombinant human NPPA, expressed in E. coli, is a single-chain polypeptide without any glycosylation modifications. It consists of 106 amino acids, encompassing the sequence from position 26 to 123, and includes an 8-amino acid histidine tag attached to the N-terminus. The calculated molecular weight of this protein is 11.7 kDa.

Shipped with Ice Packs
Cat. No.
BT19388
Source
Escherichia Coli.
Appearance
The product appears as a white, lyophilized (freeze-dried) powder after filtration.

NPPC Human

Natriuretic Peptide C Human Recombinant

Recombinant human NPPC, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 126 amino acids (residues 24-126) with a molecular weight of 13.2 kDa. This protein encompasses amino acids 24 to 126 of the NPPC sequence and incorporates a 23-amino acid His-tag at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19462
Source
Escherichia Coli.
Appearance
Clear solution subjected to sterile filtration.

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 (amino acids 1-85) containing 101 amino acids. It has a molecular mass of 10,545 Daltons. This NT-proBNP is fused with a 16 amino acid affinity tag at the N-terminus and purified using 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

Recombinant Human NT-Pro-B-type Natriuretic Protein, produced in E. coli, is a polypeptide chain without any sugar molecules attached (non-glycosylated). It comprises 76 amino acids and has a molecular weight of about 8.5 kDa.

The purification of NT-proBNP is achieved through specific chromatographic methods.

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, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising amino acids 1-108. It is fused to a His-tag and possesses a molecular weight of approximately 13 kDa. The purification of proBNP is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19713
Source

Escherichia Coli.

Appearance
Sterile Filtered colorless liquid.
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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