Search results
This is an online tool for protein extinction coefficient (280nm and 214nm) and concentration calculation. Please input the amino acid sequence of your protein in the text-box below. Protein complex can be treated as a single chain protein, for example, if the complex consists of two A chains and one B chain, then just enter the sequence of A+A ...
13 gru 2016 · For a typical IgG with MW = 150,000, this value corresponds to a molar extinction coefficient (ε) equal to 210,000 M-1cm-1. The typical ϵ percent or A percent 280nm used for the nanodrop for IgGs is A 1% 280 nm = 13.7 or A 0.1% 280nm = 1.37.
The concentration of IgG in solution can be determined by substituting the molecular weight, extinction coefficient and λ max into a derived form of the Beer - Lambert Law. A substance's λ max is the wavelength at which it experiences the strongest absorbance. For IgG, this wavelength is 280 nm.
Without also knowing the extinction coefficient for the proteins in the sample, you will not know whether the same concentrations of BSA and sample protein will have the same absorbance. (For example, 1mg/mL IgG has nearly twice the absorbance of 1mg/mL BSA.)
The absorptivity coefficient, also known as the extinction coefficient ( ε ), can be established for any given protein. For each protein or peptide, the extinction coefficient can
Assuming a standard 1cm pathlength cuvette (εmolar L)/MW is sometimes simplified to ε0.1% the mass extinction coefficient or the percent solution extinction coefficient (absorbance values at 280nm for a 0.1% solution of a reference protein measured in a 1cm cuvette with units (mg/mL)-1 cm-1).
8 kwi 2024 · Let's say we need to find out the concentration of an Immunoglobin G (IgG) sample, which has an extinction coefficient of 210,000 M⁻¹ cm⁻¹ and a molecular weight of 150,000 g/mol. Insert the wavelength at which you measured the maximum absorption.
