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- 2025年07月09日
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文献和实验Determination of Epitopes by Mass Spectrometry
located on the gp41 protein of the human immunodeficiency virus recognized by the monoclonal antibody 2F5. In this approach we coupled the antigen SOSgp140 to the antibody 2F5, which was covalently linked to an Fc-specific antibody immobilized on cyanogen
Expression of Recombinant Proteins with Uniform N-Termini
to a self-splicing mini-intein. This fusion construct is expressed in an engineered E. coli strain from which the pepP gene coding for aminopeptidase P has been deleted. We describe a protocol using human cationic trypsinogen as an example to demonstrate
Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli
(1 ). Recombinant proteins produced in E. coli sometimes retain the N-terminal initiator methionine residue, as they may be a poor substrate for the host methionine aminopeptidase (2 ). In addition, individual purification schemes must be devised for each native
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