Literature DB >> 9368641

Simple affinity purification of antibodies using in vivo biotinylation of a fusion protein.

S A Lesley1, D J Groskreutz.   

Abstract

We describe a method for affinity purification of antibodies using gene fusions to the antigen. Fusions are made to a protein domain which is recognized in vivo by biotin ligase and biotinylated at a unique position in the fusion protein. When expressed in E. coli, the fusion protein can be captured from a whole cell lysate using an avidin resin to generate an affinity column which is useful for antibody purification. The procedure is simple, rapid and does not require chemical biotinylation or prior purification of the target antigen.

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Year:  1997        PMID: 9368641     DOI: 10.1016/s0022-1759(97)00113-0

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  2 in total

1.  Development of the "Three-step MACS": a novel strategy for isolating rare cell populations in the absence of known cell surface markers from complex animal tissue.

Authors:  Mathia Y Lee; Thomas Lufkin
Journal:  J Biomol Tech       Date:  2012-07

2.  Supported Lipid Bilayer Technology for the Study of Cellular Interfaces.

Authors:  Travis J Crites; Michael Maddox; Kartika Padhan; James Muller; Calvin Eigsti; Rajat Varma
Journal:  Curr Protoc Cell Biol       Date:  2015-09-01
  2 in total

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