With plans to conjugate a protein to antibody, previous attempts, via amine linkage on one end (the antibody) and maleimide coupling on the other end (via a cysteine residue on my protein), the results were not optimal. More reproducible results and more control of the process is desired, specifically with less proteins conjugated to each antibody, ideally a 1:1 ratio. Considering attachment of the protein cysteine to carbohydrate on the antibody. I notice you have reagents that can couple to cysteine via maleimide, do you have a reagent that oxidizes carbohydrate groups and also a linker that couples to the resultant aldehydes?

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We cannot recommend the scheme proposed. The way we typically conjugate through the carbohydrate groups is by oxidation, which would give one less control, not more, and the oxidative product is an aliphatic aldehyde, which is not as stable as the aromatic aldehyde. We get very controllable, reproducible results with our UV- traceable chemistry that links through the amino groups.