Amid Biosciences| Competent Cells and Protein Expression Vectors
Phage Display ER2738 Electrocompetent E. coli Cells | Amid Biosciences
The E. coli strain ER2738 is an amber suppressor (glnV) F+ strain with a rapid growth rate and is particularly well-suited for M13 phage propagation. Amid Biosciences’ high efficiency electrocompetent ER2738 cells can be used for phage display, antibody phage display, library construction and screening. The F-factor of ER2738 contains a mini-transposon which confers tetracycline resistance, so cells can be selected by plating and propagating in tetracycline-containing medium. ER2738 cultures for infection can be grown either in LB or LB+Tet media. Tetracycline does not need to be added to media during phage amplification. Loss of F-factor in nonselective media is insignificant as long as cultures are not serially diluted. Although ER2738 is a recA+ strain, there are no reports on spontaneous in vivo recombination events with M13 or phagemid vectors.
ER2738 cells are recommended for use with New England Biolab′s Ph.D.™ Phage Display Kits (1). ER2738 electrocompetent E. coli cells are supplied as a pack of 10 convenient 50 µl per tube aliquots (sufficient for 20 reactions).
Bulk quantities and custom packaging are available at very competitive prices for all Competent Cells.
Catalog # EREC-201
F´proA+B+ lacIq Δ(lacZ)M15 zzf::Tn10(TetR)/ fhuA2 glnV Δ(lac-proAB) thi-1 Δ(hsdS-mcrB)5
Features and Benefits
- Transformation efficiency > 1010 transformants /µg pBR322
- Useful for preparation of phage display libraries
- Amber suppressor (supE): UAG>CAG(Gln)
Storage: at -80°C.
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Usage: This product is intended for LABORATORY RESEARCH USE ONLY. Not for diagnostic or therapeutic use.
2. Tjhung K. et al. Intra-domain phage display (ID-PhD) of peptides and protein mini-domains censored from canonical pIII phage display. Front. Microbiol., 28 April 2015 | https://doi.org/10.3389/fmicb.2015.00340
3. Qiang X. et al. Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization. Scientific Reports, volume 7, Article number: 2673 (2017)