The full-length pre-proBNP (134 aa) is cleaved into proBNP (1-108), which is further processed into:
BNP (27-102) spans a portion of proBNP but lacks the mature BNP (77-108) sequence. It retains structural motifs relevant for antibody binding in diagnostic assays .
Expressed in E. coli with an N-terminal His tag for purification .
Lyophilized without additives; reconstituted in sterile water or buffers containing 0.1% BSA .
Used as an antigen to generate antibodies for BNP immunoassays .
Critical for standardizing assays measuring NT-proBNP and proBNP in heart failure diagnostics .
Investigates proBNP processing enzymes (e.g., corin, furin) and degradation pathways .
Helps identify cross-reactive epitopes in commercial BNP tests, improving assay specificity .
Prognostic Marker: Elevated BNP levels correlate with heart failure severity and mortality .
Therapeutic Target: Recombinant BNP analogs (e.g., nesiritide) mimic endogenous BNP’s vasodilatory effects .
Heterogeneity: ProBNP exists as glycosylated and oligomerized forms, complicating assay accuracy .
Stability: BNP (27-102) requires stringent storage conditions to maintain integrity .
Natriuretic Peptide Precursor B, also known as BNP, is a cardiac hormone with various biological effects. These include promoting the excretion of sodium and water (natriuresis and diuresis), relaxing blood vessels (vasorelaxation), and inhibiting the production of renin and aldosterone. BNP is believed to be crucial for maintaining cardiovascular balance, restoring the body's salt and water equilibrium, and enhancing heart function.
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).
The BNP product is filtered (0.4 µm) and lyophilized from a solution containing 0.5mg/ml BNP, 20 mM Tris buffer, and 50 mM NaCl at a pH of 7.5.
To create a working stock solution, add deionized water to the lyophilized pellet until it reaches a concentration of approximately 0.5mg/ml. Allow the pellet to fully dissolve. Please note that this BNP product is not sterile. Before using it in cell culture, filter it through a suitable sterile filter.
The purity of this product is greater than 95.0% as determined by SDS-PAGE analysis.
NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.
MKHHHHHHPL GSPGSASDLE TSGLQEQRNH LQGKLSELQV EQTSLEPLQE SPRPTGVWKS REVATEGIRG HRKMVLYTLR APR.
BNP functions as a cardiac hormone with multiple biological actions critical to cardiovascular function:
Natriuresis and diuresis (promoting sodium and water excretion)
Vasorelaxation (dilating blood vessels to reduce blood pressure)
Inhibition of renin and aldosterone secretion (modulating the renin-angiotensin-aldosterone system)
Restoration of salt and water balance
These physiological roles make BNP an important research target for understanding cardiovascular pathophysiology and developing therapeutic interventions for heart failure and hypertension.
Research has demonstrated significant associations between BNP levels and clinical outcomes, particularly mortality. A 2024 study of 3,220 critically ill pediatric patients revealed:
This relationship was non-linear, with log2 BNP associated with increased risk (OR 1.28, 95% CI 1.19-1.38; P < 0.001). Subgroup analyses further revealed that very high BNP levels were especially significant in infants, patients with lactate ≥ 2.0 mmol/L, or CKMB ≥ 45 μ/L .
Patient Group | BNP Threshold | Adjusted Mortality Odds Ratio | 95% Confidence Interval | P-value |
---|---|---|---|---|
All patients | ≥ 10,170 pg/ml | 2.017 | 1.265-3.217 | 0.0032 |
When investigating BNP gene expression in response to mechanical stress, researchers should consider both acute and chronic models:
For acute mechanical stress:
Vasopressin (AVP) infusion can be used to create increased cardiac workload
Study the involvement of secondary messengers such as angiotensin II (Ang II) and endothelin-1 (ET-1) in the early activation of BNP gene expression
Monitor hemodynamic parameters simultaneously to correlate with gene expression changes
For chronic mechanical stress:
Spontaneously hypertensive rats (SHR) provide a genetic model of cardiac overload
Analyze both ventricular BNP gene expression and peptide levels to capture transcriptional and translational changes
Include time-course experiments to distinguish between early and late adaptive responses
Methodological recommendations include:
Use of quantitative PCR for gene expression analysis
Radioimmunoassay or ELISA for peptide quantification
In situ hybridization to localize expression within cardiac tissues
Parallel analysis of other natriuretic peptides (ANP, CNP) for comprehensive understanding
For researchers seeking to quantify BNP (27-102) Human in experimental samples, enzyme-linked immunosorbent assay (ELISA) remains the gold standard:
Sandwich ELISA approach:
Sample preparation considerations:
Minimize freeze-thaw cycles to prevent protein degradation
Consider potential matrix effects from different sample types (serum, plasma, cell culture)
Include appropriate calibration curves using recombinant human Pro-BNP
Validation parameters:
Determine assay sensitivity (lower limit of detection)
Establish specificity through cross-reactivity studies
Assess precision through intra- and inter-assay coefficient of variation
Confirm linearity across the expected concentration range
Commercial kits are available but researchers may develop custom assays for specific research needs. When developing custom assays, antibody pair selection and optimization of blocking conditions are critical for assay performance.
While BNP was initially studied primarily in relation to cardiac diseases, recent research has expanded our understanding of its significance in non-cardiac conditions:
The 2024 pediatric intensive care study demonstrated BNP's association with all-cause mortality, including in children with non-cardiac diseases
This suggests BNP may serve as a broader biomarker of physiological stress beyond cardiac-specific pathology
When interpreting BNP data in non-cardiac conditions, researchers should:
Control for potential confounding factors:
Age (especially important in pediatric populations)
Renal function (impaired kidney function affects BNP clearance)
Inflammatory status (inflammation may alter BNP expression)
Body mass index (inverse relationship with natriuretic peptide levels)
Consider analytical approach:
Apply multivariate analysis to adjust for covariates
Utilize non-linear statistical models, as the BNP-outcome relationship is often non-linear
Determine appropriate cutoff values specific to the population and condition under study
Context-specific interpretation:
Higher baseline levels may be expected in elderly populations
Different reference ranges may apply for different clinical conditions
Serial measurements may provide more valuable information than single time point values
Selection of appropriate experimental models is crucial for advancing BNP research:
Model Type | Applications | Advantages | Limitations |
---|---|---|---|
Spontaneously hypertensive rats (SHR) | Hypertension studies, chronic cardiac overload | Genetic model with gradual progression, mimics human hypertension | Strain-specific effects may limit generalizability |
Acute hemodynamic overload models | Study of immediate BNP responses | Controlled conditions, reproducible | May not capture chronic adaptive changes |
Cell culture systems (cardiomyocytes) | Molecular mechanisms, signal transduction | Isolated cellular responses, easily manipulated | Lacks systemic interactions |
Ex vivo heart preparations | Direct mechanical stress studies | Maintains tissue architecture, allows precise hemodynamic control | Limited viability duration |
Clinical samples | Translational research | Direct human relevance | Variability, ethical considerations, limited availability |
When designing studies using these models, researchers should:
Match the model to the specific research question
Include appropriate controls for each model system
Consider potential species differences in BNP processing and signaling
Validate findings across multiple model systems when possible
The non-linear relationship between BNP and mortality has important implications for experimental design:
Statistical analysis considerations:
Sampling strategy:
Ensure adequate representation across the entire BNP concentration range
Increase sampling density around identified threshold points (e.g., 10,170 pg/ml in the pediatric population)
Consider stratified analysis across different BNP ranges
Subgroup considerations:
B-type Natriuretic Protein (BNP), also known as B-type Natriuretic Peptide, is a hormone produced by the heart. It plays a crucial role in cardiovascular homeostasis by regulating blood pressure, fluid balance, and electrolyte levels. The specific form, B-type Natriuretic Protein (27-102 a.a.) (Human Recombinant), refers to a recombinant version of the protein that includes amino acids 27 to 102 of the human BNP sequence.
BNP was first discovered in brain tissue, which is why it is sometimes referred to as “brain” natriuretic peptide . However, it is predominantly produced by the ventricular myocardium of the heart . The protein is initially synthesized as a preprohormone, which is then cleaved to form the active hormone. The active form of BNP consists of 32 amino acids, but the recombinant version often includes additional amino acids for stability and activity.
BNP has several important biological functions:
BNP levels are commonly measured in clinical settings to diagnose and manage heart failure. Elevated levels of BNP in the blood are indicative of heart failure, as the heart releases more BNP in response to increased pressure and volume load . The BNP test is a valuable tool for distinguishing between heart failure and other conditions that cause similar symptoms, such as pneumonia .
Recombinant BNP, such as B-type Natriuretic Protein (27-102 a.a.) (Human Recombinant), is produced using recombinant DNA technology. This involves inserting the gene encoding BNP into a host organism, such as bacteria or yeast, which then produces the protein. Recombinant BNP is used in research and therapeutic applications, including the treatment of acute heart failure.