Sheldon Park, PhD, University at Buffalo — Published: August 27, 2013

Streptavidin is widely used in biotechnology and molecular research for detection, purification, crosslinking, and labeling of biotinylated targets. However, wild-type streptavidin is an obligate tetramer and can crosslink biotinylated targets. Target aggregation is a significant obstacle in some applications, including the labeling of biotinylated cell surface receptors, where crosslinking can perturb protein stability and function. This Engineered Monomeric Streptavidin 2 (mSA2) allows for aggregation-free association with biotinylated ligands and can be used as a genetic fusion tag.

Source: Wiley Video Abstract, Biotechnology and Bioengineering DOI: 10.1002/bit.24605

Learn more about the Engineered Monomeric Streptavidin 2 (mSA2) Protein »

Tags:

Streptavdin, Biotin, Streptavidin-biotin, Affinity purification, Engineered Monomeric Streptavidin 2 (mSA2) Protein

References:

1. Lim, K.H., Huang, H., Pralle, A., and Park, S. Stable, High-Affinity Streptavidin Monomer for Protein Labeling and Monovalent Biotin Detection. Biotechnology Bioeng 110, 57-67 (2013)
2. DeMonte, D., Drake, E., Lim, K.H., Gulick, A., Park, S., Structure based engineering of streptavidin monomer with a reduced biotin dissociation rate. Proteins: Structure, Function, and Bioinformatics (DOI: 10.1002/prot.24320)