Reagents to modify proteins by crosslinking, fragmenting, denaturing, reducing disulfides, or attaching various prosthetic groups (e.g. PEGylation) to allow manipulation and study of protein function and interactions in any environment.

Featured protein modification reagents

Chemical agents to modify amino acid side chains on proteins and peptides in order to alter charges, block or expose reactive binding sites, inactivate functions, or change functional groups to create targets for crosslinking and labeling.

Activated linear and branched derivatives of polyethylene glycol (PEG) for pegylation and PEG-modification of peptides and proteins via primary amines and sulfhydryl groups to increase solubility, prolong stability, and reduce immunogenicity.

Purified and agarose-immobilized proteases for the enzymatic proteolysis (cleavage or digestion) of proteins to facilitate amino acid sequencing, peptide analysis, and polypeptide structural characterization.

Chaotropic and denaturing chemical agents, including urea and guanidine hydrochloride, disrupt water interactions and promote hydrophobic protein and peptide solubilization, elution, refolding, and structural analysis.

Purified powders, convenient solutions, and solid-phase resins of disulfide reducing agents, including DTT, BME and TCEP, for stabilizing free sulfhydryls (cysteines) and reducing disulfide bonds.

Protein quantitation immunoassays
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