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Protein Concentration Calculator

Calculate protein concentration from spectrophotometer absorbance data using the Beer-Lambert Law

Calculate Protein Concentration

Extinction Coefficient: 210,000 M⁻¹ cm⁻¹

Molecular Mass: 150,000 g/mol

Enter 1 for stock solution, 2 for 1:2 dilution, etc.

Protein Concentration Results

0.000e+0
mg/mL
0.000e+0
µg/mL
0.000e+0
Molar (M)

Formula used: C = (A / (ε × b)) × M × n

Parameters: Absorbance: 0, Extinction Coeff: 210000 M⁻¹ cm⁻¹, Pathlength: 1.00 cm

Protein: IgG – Immunoglobin G (MW: 150000 g/mol)

Example Calculation

IgG Protein Analysis Example

Protein: IgG (Extinction coefficient: 210,000 M⁻¹ cm⁻¹, Molecular mass: 150,000 g/mol)

Absorbance: 0.5 at 280 nm

Pathlength: 1 cm

Dilution factor: 10 (1:10 dilution)

Calculation

C = (A / (ε × b)) × M × n

C = (0.5 / (210,000 × 1)) × 150,000 × 10

C = 3.571 mg/mL

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💡 Key Points

Proteins typically absorb at 280 nm wavelength

Standard cuvette pathlength is 1 cm

Account for dilution factor in your measurements

Higher extinction coefficients give more sensitive measurements

Clean cuvettes are essential for accurate readings

📚 Common Proteins

BSA

Bovine Serum Albumin

Most common protein standard

IgG

Immunoglobulin G

Common antibody protein

LYS

Lysozyme

Antimicrobial enzyme

Understanding Protein Concentration Calculation

The Beer-Lambert Law

The protein concentration calculator is based on the Beer-Lambert Law, which describes the absorption of light by molecules in solution:

A = ε × b × C

Rearranged for concentration:

C = A / (ε × b)

For proteins, we multiply by molecular mass and dilution factor to get mass concentration in mg/mL.

Parameters Explained

Absorbance (A)

Optical density measured by spectrophotometer, typically at 280 nm for proteins

Extinction Coefficient (ε)

Protein-specific constant describing light absorption strength (M⁻¹ cm⁻¹)

Pathlength (b)

Inner diameter of the cuvette, usually 1 cm for standard cuvettes

Molecular Mass

Atomic mass of the protein in grams per mol (g/mol)

Dilution Factor

Accounts for sample dilution (1 for stock, 2 for 1:2 dilution, etc.)

Measurement Methods

UV Spectrophotometry

Direct measurement of protein absorbance at 280 nm. Most accurate for pure proteins.

Bradford Assay

Colorimetric method using Coomassie dye. Good for protein mixtures and low concentrations.

BCA Assay

Bicinchoninic acid method. Compatible with most detergents and reducing agents.

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