Chemical agents used to modify the amino acid side chains of proteins in order to alter their native charges, block or expose reactive binding sites, inactivate functional groups, and change functional groups to create targets for crosslinking and labeling.
Remove fusion tags from proteins with the HRV 3C cleavage sequence with this recombinant cysteine protease that is dual tagged for easy removal from the sample after cleavage.
Reduce protein and peptide disulfide bonds using this thiol-free, pure, crystalline tris (2-carboxyethyl) phosphine hydrochloride, TCEP (CAS 5961-85-3).
Highly active serine protease that exhibits broad cleavage specificity on native and denatured proteins and is widely used in the purification of DNA and RNA
Efficiently reduce protein or peptide disulfide bonds with this reusable column on with an immobilized thiol-based reducing agent for solid-phase disulfide bond reduction.
CA(PEG)n: pegylated amino acids of the form carboxy-PEG-amine; with 4 to 24 polyethylene glycol units; for surface- and molecule-pegylation applications.
Cleave at the carboxyl-side of aliphatic, aromatic or hydrophobic residues and digest-inactivate DNase and RNase in nucleic acid purification using this protease.