BL21(λDE3) pLPP – Lambda Protein Phosphatase Co-Expression System | Production of Unphosphorylated Proteins
BL21(λDE3) pLPP – Lambda Protein Phosphatase Co-Expression System | Production of Unphosphorylated Proteins
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Undesired phosphorylation of proteins can be observed during expression in various strains due to either phosphorylation by host kinases or autophosphorylation.
The BL21(λDE3) pLPP is an E. coli strain that is developed for high-efficiency expression of homogeneously non-phosphorylated proteins including both serine/threonine kinases and tyrosine kinases. The BL21(λDE3) pLPP competent cells contain an IPTG-inducible bacteriophage lambda protein phosphatase (lambda PP) expression plasmid. Lambda protein phosphatase is highly specific enzyme that removes phosphorylation from Ser, Thr, and Tyr residues in proteins (1-3). The lambda PP plasmid carries the resistance gene for streptomycin/spectinomycin and is compatible for co-expression with many E. coli and T7 promoter driven vectors (pET, pTrc, and etc).
Amid Biosciences BL21(λDE3) pLPP chemically competent cells are supplied as a pack of 10 convenient 100 μl/tube aliquots.
Catalog # BLPP-201
This product is intended for laboratory research use only.
Transformation efficiency: >1 x 10^4 cfu/µg pBR322
E. coli genotype: fhuA2 [lon] ompT gal (λ DE3) [dcm] ∆hsdS pLPP (StrR) [λDE3 = λ sBamHIo ∆EcoRI-B int::(lacI::PlacUV5::T7 gene1) i21 ∆nin5]
Storage: at -80°C
References:
- Bhoir, S., Shaik, A., Thiruvenkatam, V. et al. High yield bacterial expression, purification and characterization of bioactive Human Tousled-like Kinase 1B involved in cancer. Sci Rep 8, 4796 (2018). https://doi.org/10.1038/s41598-018-22744-5
- Zhuo, S. et al., Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. J. Biochem., 1993, 268, 17754-17761.
- Shrestha, A. et al. Analysis of conditions affecting auto-phosphorylation of human kinases during expression in bacteria. Protein Exp. and Purification, 2012, 81 (1), 136-143. https://doi.org/10.1016/j.pep.2011.09.012
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