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Purification of IgG Antibody from Human Serum

Shahid Afridi^*

Department of Clinical Science, BS Abdur Rahman Crescent Institute of Science and Technology, Vandalur, Chennai, India

Received Date: Mar 19, 2022 / Published Date: May 27, 2022

Citation: Afridi S (2022) Purification of IgG Antibody from Human Serum. J Clin Exp Pathol 12:410.

Copyright: © 2022 Afridi S. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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In present world monoclonal and polyclonal antibody are widely used in medicine and therapeutics. Hence there is increase in the consumption of plasma derived Immunoglobulin G (IgG) as they are used in the treatment of number of diseases, including neurological diseases and autoimmune conditions. It is necessary to produce IgG derived plasma protein in high quantity to meet the rate of its consumption. Isolation of immunoglobulin in research lab for different application is from cell culture medium, plasma, serum, hybrid cell etc. There are various methods like ammonium sulphate precipitation, affinity chromatography and thiophilic chromatography to purify the desired antibody from human serum sample. Depending upon the biochemical properties of immunoglobulin, different chromatographic techniques are performed to isolate antibody from the source sample. In our present investigation we have purified IgG antibody from human serum sample using protein-An affinity chromatography. After each purification step the biuret test was taken to quantify the protein concentration. The protein a purified sample weighs 5 mg/ml after dialysis was analyzed along with a standard protein marker in polyacrylamide gel electrophoresis. The molecular weight of protein a purified IgG was found in between 20 kda to 90 kda after SDS-PAGE analysis.

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