1. What is BSA Concentration?

BSA (Bovine Serum Albumin) concentration is commonly measured in laboratory settings using spectrophotometry and the Beer-Lambert law. This calculation helps researchers quantify protein concentrations in their samples.

2. How Does the Calculator Work?

The calculator uses the Beer-Lambert law:

Where:

• \( A \) — Absorbance (unitless, typically at 280 nm)
• \( \varepsilon \) — Extinction coefficient (6.6 mL/mg·cm for BSA at 280 nm)
• \( l \) — Path length of the cuvette (usually 1 cm)

Explanation: The equation relates the absorption of light to the concentration of the absorbing substance in solution.

3. Importance of BSA Measurement

Details: Accurate BSA concentration measurement is crucial for protein quantification, standardization of experiments, and preparation of calibration curves in biochemical assays.

4. Using the Calculator

Tips:

• Enter absorbance value (typically between 0.1-1.0 for accurate measurements)
• Default extinction coefficient is 6.6 mL/mg·cm for BSA at 280 nm
• Standard path length is 1 cm (adjust if using different cuvette)

5. Frequently Asked Questions (FAQ)

Q1: Why use 280 nm for BSA measurement?
A: BSA absorbs strongly at 280 nm due to its tryptophan and tyrosine content, making this wavelength ideal for quantification.

Q2: What if my sample absorbance is too high?
A: For absorbance >1.0, dilute your sample and multiply the result by the dilution factor for accurate measurement.

Q3: Can I use this for other proteins?
A: Yes, but you'll need the specific extinction coefficient for your protein of interest.

Q4: How accurate is this method?
A: Very accurate when performed correctly, but affected by sample turbidity, impurities, and pH variations.

Q5: What's the typical BSA concentration range?
A: Working concentrations typically range from 0.1 mg/mL to 10 mg/mL, depending on application.