pRSET-mSA2 Protein Expression Vector
This expression vector contains the core domain of mSA2 following an N-terminal 6xHis tag. The purification tag may be removed using TEV to yield mSA2 fused to a C-terminal FLAG tag.
mSA2 Highlights:
- Monomeric form allows for association with biotinylated ligands without inducing aggregation through multivalent interaction
- Smaller MW compared to wild type streptavidin is advantageous in applications where access to biotinylated ligands may be a concern
- Moderate affinity for biotin compared to wild-type strepavidin useful for subsequent dissociation of the bound ligand
- Can be used as a genetic fusion tag, in which mSA2 can be fused to cell surface receptors and labeled with biotinylated fluorophores
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.
From the laboratory of Sheldon Park, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
This expression vector contains the core domain of mSA2 following an N-terminal 6xHis tag. The purification tag may be removed using TEV to yield mSA2 fused to a C-terminal FLAG tag.
mSA2 Highlights:
- Monomeric form allows for association with biotinylated ligands without inducing aggregation through multivalent interaction
- Smaller MW compared to wild type streptavidin is advantageous in applications where access to biotinylated ligands may be a concern
- Moderate affinity for biotin compared to wild-type strepavidin useful for subsequent dissociation of the bound ligand
- Can be used as a genetic fusion tag, in which mSA2 can be fused to cell surface receptors and labeled with biotinylated fluorophores
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.
From the laboratory of Sheldon Park, PhD, University at Buffalo.
Part of The Investigator's Annexe program.
| Product Type: | Plasmid |
| Gene/insert name: | Monomeric Streptavidin (mSA) 2 |
| Accession ID: | P22629 |
| Antibiotic Resistance: | Ampicillin |
| Fusion Tag(s): | 6xHis (N terminal on backbone), TEV (N terminal on insert), FLAG (C terminal on backbone) |
| Grow in E. coli at 37 C: | Yes |
| Selectable markers: | None |
| Cloning Site 5': | NheI |
| Cloning Site 3': | XhoI |
| Insert Size: | 378 bp |
| Vector Backbone and Size: | pRSETA, 3566 bp |
| High or low copy: | High |
| Storage: | Store at -20C |
| Shipped: | Ambient temperature |
pRSET-mSA2 Vector Map
- 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)
- DeMonte, D., Drake, E., Lim, K.H., Gulick, A., Park, S., Structure based engineering of streptavidin monomer with a reduced biotin dissociation rate. Proteins. 2013 Sep;81(9):1621-33.
- Lim KH, Huang H, Pralle A, Park S. Engineered streptavidin monomer and dimer with improved stability and function. Biochemistry. 2011 Oct 11;50(40):8682-91.
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