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Related Concept Videos

Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: Jul 2, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins
07:44

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

A simple high-throughput purification method for hit identification in protein screening.

Emma Cummins1, Deborah P Luxenberg, Fionnuala McAleese

  • 1Wyeth Research Ireland, Conway Institute of Biomolecular and Biomedical Research, University College Dublin, Belfield, Dublin, Ireland. cummine4@wyeth.com

Journal of Immunological Methods
|September 2, 2008
PubMed
Summary
This summary is machine-generated.

High-throughput protein purification for pharmaceutical screening is streamlined using the HIS-Select 96-well filter plate system. This method efficiently produces high-purity single-chain variable fragments (scFvs) for functional assays.

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10:02

Identification of Protein Interacting Partners Using Tandem Affinity Purification

Published on: February 25, 2012

Area of Science:

  • Biotechnology
  • Protein Engineering
  • Pharmaceutical Development

Background:

  • Phage and ribosome display are crucial for high-throughput screening of protein pharmaceuticals.
  • Purifying large protein quantities is a significant challenge for these screening methods.
  • Functional and cell-based assays often demand high-purity and concentrated proteins.

Purpose of the Study:

  • To evaluate and optimize small-scale, high-throughput protein purification methods.
  • To assess the suitability of the HIS-Select 96-well filter plate system for protein purification.
  • To validate the purity and functionality of purified proteins in cell-based assays.

Main Methods:

  • Evaluation of various small-scale protein purification techniques.
  • Optimization of the HIS-Select 96-well filter plate system.
  • Production and purification of single-chain variable fragments (scFvs) using the optimized method.
  • Testing purified scFvs in cell-based functional assays.

Main Results:

  • The HIS-Select 96-well filter plate system was identified as the preferred method for high-throughput purification.
  • Optimized HIS-Select purification yielded 50-100 microg of scFvs with sufficient purity for cell-based assays.
  • Purified scFvs demonstrated similar functional behavior to those purified by traditional large-scale methods.
  • The method facilitates purification of large numbers of IgGs and Fc fusion proteins.

Conclusions:

  • The HIS-Select 96-well filter plate system offers an efficient solution for high-throughput protein purification.
  • This method enables the evaluation of numerous proteins, including scFvs, IgGs, and Fc fusion proteins, in functional assays.
  • The optimized protocol supports the advancement of protein pharmaceutical discovery and development.