Labeling experiments for protein expression
Most proteins are prepared using recombinant expression techniques. During the cloning process, additional residues or tags can be added to the N- or C-terminus
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Protein concentration and solute removal experiments
Outstanding growth is expected in novel primary molecules and biosimilar entities. Some of the advances are improved analysis, development and interactions. Num
Maintenance of protein stability
This method is mainly used to maintain the stability of proteins.
Bacterial expression systems for exogenous protein production
Bacterial expression systems are available in a wide variety of vectors and host bacteria, and the short proliferation time of most engineered bacteria not only
Gel filtration experiment
Unique among chromatographic techniques for protein purification, gel filtration separates proteins based on the relative size of their molecular masses. In con
Identification, production and use of polyhydroxy-reactive monoclonal antibodies - for immunoaffinity chromatography
All forms of affinity chromatography require the formation of a specific interaction between two components by which one of the components can be purified. Immu
Isoelectric spot focusing for protein separation
Proteins can be separated on coated or uncoated capillary columns, and the choice of separation protocol depends on the specific properties of the target protei
Preparation of monoclonal antibodies against phosphopeptides.
This experiment provides steps starting from inoculation of candidate hybridoma clones into a 96-well culture plate all the way through to isolation of a hybrid
Determination of phosphorylated amino acid positions in peptides
If the sample volume is insufficient for direct sequencing, the peptide can be degraded by manual Edman degradation to determine the location of the phosphoryla