Protein concentration from A280

Protein concentration from absorbance at 280 nm follows Beer–Lambert: mg/ml = A280 × MW / ε, with ε the molar extinction coefficient (M⁻¹cm⁻¹) and a 1 cm path. For BSA (ε 43,824, MW 66,463) an A280 of 1.0 is 1.52 mg/ml. Tryptophan, tyrosine and cystines are what absorb — ε is protein-specific.

M⁻¹cm⁻¹
g/mol
×

Result

Concentration1.517mg/ml
Molar concentration22.82µM

Beer–Lambert: mg/ml = A280 × MW / ε; µM = A280/ε × 10⁶. Defaults are BSA (ε 43,824 M⁻¹cm⁻¹, MW 66,463 Da per ExPASy ProtParam). Get ε for your protein from its sequence — Talindrew's protein tools compute it by the Pace 1995 method.

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Formula

c (mg/ml) = A280 × MW / ε · c (µM) = A280 / ε × 10⁶

Source: Beer–Lambert law; ε predicted from sequence per Pace et al., Protein Sci 1995

Worked example

Given: BSA solution, A280 = 1.0 (ε 43,824 M⁻¹cm⁻¹, MW 66,463 Da per ProtParam)

  1. 1.Molar concentration: 1.0 / 43,824 = 22.8 µM.
  2. 2.Mass concentration: 1.0 × 66,463 / 43,824 = 1.52 mg/ml.

A280 1.0 of BSA = 1.52 mg/ml (22.8 µM)

How the calculation flows

Protein concentration from A280 — calculation flowBeer–Lambert with a protein-specific extinction coefficient: dividing by ε gives molarity; multiplying by MW gives mass concentration.A2801 cm path÷ εprotein-specific× MWg/molmg/mland µM
Beer–Lambert with a protein-specific extinction coefficient: dividing by ε gives molarity; multiplying by MW gives mass concentration.

Units & constants

What absorbs at 280 nmTrp (ε ~5,500) ≫ Tyr (~1,490) > cystine (~125) per residue
ε predictionPace 1995 method from sequence (ProtParam; Talindrew protein tools)
BSA referenceε 43,824 M⁻¹cm⁻¹, MW 66,463 Da
Lysozyme referenceε 37,970 M⁻¹cm⁻¹, MW 14,313 Da
Reliable A280 range~0.1–1.0; dilute and multiply back
CaveatNucleic acid contamination inflates A280 (check A260/A280)
PriceFree

Where do you get ε for your protein?

Compute it from the sequence: the Pace 1995 method sums contributions of tryptophans, tyrosines and disulfide-bonded cystines, and is what ExPASy ProtParam and Talindrew's protein properties report. Use the value matching your protein's state — reduced (free cysteines) or with disulfides formed — they differ by 125 M⁻¹cm⁻¹ per cystine.

When is A280 the wrong method?

A280 fails predictably in a few cases:

  • Proteins with no Trp/Tyr (some small peptides): ε is tiny and the reading is noise — use BCA or Bradford.
  • Crude lysates: everything absorbs; A280 reads total aromatic content, not your protein.
  • Detergent- or nucleotide-containing buffers: background absorbance shifts — always blank with the exact buffer.
  • Nucleic acid contamination: DNA absorbs strongly at 280 too; an A260/A280 above ~0.7 for a pure protein flags trouble.

Frequently asked questions

What is the old 'A280 of 1 = 1 mg/ml' rule?
A rough average (ε/MW ≈ 1 (mg/ml)⁻¹cm⁻¹) that happens to be nearly right for antibodies (IgG: 1.35–1.4) and wrong by up to two-fold for many proteins. With a computed ε there is no reason to use it.
Does the calculator handle diluted samples?
Yes — enter the dilution factor and the result is scaled back to the stock concentration, the same convention as the OD260 nucleic-acid calculator.

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