CMC0019
OverExpress™ C43(DE3) Chemically Competent Cells
Escherichia coli, rod shaped
Synonym(s):
C43 strain
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About This Item
UNSPSC Code:
41106202
NACRES:
NA.85
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product name
OverExpress™ C43(DE3) Chemically Competent Cells, for the highest protein expression
biological source
Escherichia coli
grade
for molecular biology
growth mode
adherent or suspension
morphology
rod shaped
technique(s)
microbiological culture: suitable
cell transformation
competent cell type: chemically competent
transformation efficiency: ≥1 x 106 cfu/μg
shipped in
dry ice
storage temp.
−70°C
General description
OverExpress™ Electrocompetent and Chemically Competent Cells are E. coli strains that are effective in expressing toxic proteins from all classes of organisms, including eubacteria, yeasts, plants, viruses, and mammals. The effectiveness of these new strains in expressing toxic proteins has been validated in more than 350 publications. The OverExpress™ strains contain genetic mutations phenotypically selected for conferring tolerance to toxic proteins. The strain C41(DE3) was derived from BL21(DE3). This strain has at least one mutation, which prevents cell death associated with expression of many recombinant toxic proteins. The strain C43(DE3) was derived from C41(DE3) by selecting for resistance to a different toxic protein and can express a different set of toxic proteins to C41(DE3). OverExpress™ C41(DE3)pLysS and C43(DE3)pLysS also carry a chloramphenicol-resistant plasmid that encodes T7 lysozyme, which is a natural inhibitor of T7 RNA polymerase. Cells containing pLysS produce a small amount of T7 lysozyme. These strains are used to suppress basal expression of T7 RNA polymerase prior to induction, thus stabilizing recombinants encoding particularly toxic proteins.
Genotype
F – ompT hsdSB (rB- mB-) gal dcm (DE3)
Genotype
F – ompT hsdSB (rB- mB-) gal dcm (DE3)
Application
OverExpress™ C43(DE3) Chemically Competent Cells have been used for transforming the toll/interleukin receptor (TIR) domain constructs of sterile alpha and TIR motif–containing protein 1 (SARM1).
Features and Benefits
- Express genes cloned into any T7 vector with these BL21(DE3) derivatives
- Effective in expressing toxic & membrane proteins
- Cited in over 350 research articles
Components
- OverExpress C43(DE3) chemically competent cells
- pUC 19 transformation control DNA
- recovery medium for expression
Legal Information
OverExpress is a trademark of Imaxio, S.A.
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Description
Pricing
Storage Class Code
10 - Combustible liquids
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Jia-Qi Lu et al.
International journal of molecular sciences, 22(21) (2021-11-14)
Ribosome-inactivating proteins (RIPs) hydrolyze the N-glycosidic bond and depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. In this study, we have purified and characterized lyophyllin, an unconventional RIP
Solène N Lefebvre et al.
eLife, 10 (2021-10-01)
Pentameric ligand-gated ion channels (pLGICs) mediate chemical signaling through a succession of allosteric transitions that are yet not completely understood as intermediate states remain poorly characterized by structural approaches. In a previous study on the prototypic bacterial proton-gated channel GLIC
A Rangunwala et al.
Epidemiology and infection, 142(10), 2147-2154 (2013-12-18)
Crimean-Congo haemorrhagic fever virus (CCHFV) has the propensity to cause nosocomial infections with a high fatality rate. Handling the virus requires biosafety level-4 facilities, limiting accessibility for many laboratories. Advances in molecular techniques have allowed preparation of safe recombinant antigens
Heather S Loring et al.
Bioorganic & medicinal chemistry, 28(18), 115644-115644 (2020-08-24)
Sterile Alpha and Toll Interleukin Receptor Motif-containing protein 1 (SARM1) is a key therapeutic target for diseases that exhibit Wallerian-like degeneration; Wallerian degeneration is characterized by degeneration of the axon distal to the site of injury. These diseases include traumatic
Arthur Laganowsky et al.
Nature, 510(7503), 172-175 (2014-06-06)
Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments and that lipids can bind to specific sites, for example, in potassium channels. Fundamental questions remain however regarding the extent of
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