A problem faced in proteomics studies is the recovery of tagged protein complexes in their native and active form. Here we describe a peptide, Bio-Ox, that mimics the immunoglobulin G (IgG) binding interface of Staphylococcus aureus Protein A, and competitively displaces affinity-purified Protein A fusion proteins and protein complexes from IgG-Sepharose. We show that Bio-Ox elution is a robust method for the efficient and rapid recovery of native tagged proteins, and can be applied to a variety of structural genomics and proteomics studies.

Download full-text PDF

Source
http://dx.doi.org/10.1021/pr0501517DOI Listing

Publication Analysis

Top Keywords

affinity-purified protein
8
proteomics studies
8
protein complexes
8
protein
5
method rapid
4
rapid efficient
4
efficient elution
4
elution native
4
native affinity-purified
4
protein tagged
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!