Lysis experiments with bacterial clones
Lysis experiments with bacterial clones can be used to (1) construct a phage lysogen from a recombinant phage expressing a specific fusion protein, and (2) indu
3,200+ step-by-step lab protocols and SOPs for cell culture, staining, PCR, protein work and microbiology, with reagents, conditions and evaluation criteria.
Lysis experiments with bacterial clones can be used to (1) construct a phage lysogen from a recombinant phage expressing a specific fusion protein, and (2) indu
This experiment describes the process of expressing exogenous proteins in Escherichia coli using the alkaline phosphatase promoter (phoA) and signaling sequence
This protocol is suitable for the preparation of phage progenitors, the preparation of phage particles (used to obtain DNA for subcloning), and the preparation
λ phage prepared from mass cultures can be recovered from the lysate by polyethylene glycolysis (PEG) precipitation in the presence of high salt. The residual
The exogenous protein expressed in the pGEX vector is fused to glutathione S transferase and can therefore be purified by glutathione-agarose affinity chromatog
The calcium phosphate-mediated plasmid DNA transfection of adherent cells described in this method is an improvement on the method established by Jordan et al.
Affinity chromatography methods can virtually purify maltose-binding fusion proteins into single components. Maltose-binding protein self (MBP) is a periplasmic
DNA can be well isolated from large-scale preparations of λ phage by digestion with an effective protease (e.g., proteinase K) and subsequent phenol:chloroform
This experiment was mainly used to obtain soluble active proteins.