Bispecific Purification Tag

A bispecific purification tag is an engineered peptide or protein sequence that enables selective isolation of bispecific molecules from complex biological mixtures. During purification, the tag binds a complementary ligand immobilized on a chromatography resin, allowing tagged proteins to be captured, washed to remove contaminants, and released by changing buffer conditions such as pH or ionic strength. In bispecific antibody production, this approach can simplify downstream processing, improve product recovery, and support separation of correctly assembled molecules from host-cell proteins, aggregates, or incomplete products. Purification tags therefore aid protein engineering, biomanufacturing, analytical characterization, and the development of more consistent biologic therapies.

Bispecific Purification Tag - Related Videos

Research

JoVE Journal - Biology
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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

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Cited by 7 •

2012

A novel and highly efficient two-step affinity chromatography protocol has been developed and is described in detail. The method is based on a small purification tag with two inherent affinities and is applicable to a wide range of target proteins with different properties.

Research

JoVE Journal - Biology
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High-throughput Purification of Affinity-tagged Recombinant Proteins

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Cited by 1 •

2012

We describe a method for the affinity-tagged purification of recombinant proteins using liquid-handling robotics. This method is generally applicable to the small-scale purification of soluble His-tagged proteins in a high-throughput format.

Research

JoVE EoE - Bacterial Growth and Techniques

A Procedure for the Purification of a Polyhistidine-Tagged Protein from Streptococcus mutans

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2025

Source: Murata, T., et al. Purification of a High Molecular Mass Protein in Streptococcus mutans. J. Vis. Exp. (2019)This video demonstrates a step-by-step procedure for the purification of a polyhistidine-tagged protein secreted from Streptococcus mutans.

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

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Cited by 4 •

2016

The Tandem Affinity Purification (TAP) method has been used extensively to isolate native complexes from cellular extract, primarily eukaryotic, for proteomics. Here, we present a TAP method protocol optimized for purification of native complexes for structural studies.

Evaluation of Immunomodulatory Activity of a Virally Encoded Bispecific T-Cell Engager

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2026

Source: Heidbuechel, J. P., et al. Paramyxoviruses for Tumor-targeted Immunomodulation: Design and Evaluation Ex Vivo. J. Vis. Exp. (2019).This video demonstrates a cell-based assay to evaluate the target-specific immunomodulatory activity of a virally encoded bispecific T-cell engager (BTE). The BTE links tumor cells expressing a target receptor with T cells, triggering tumor lysis and enzyme release. A colorimetric readout, based on substrate conversion, indicates T-cell activation. Higher...

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