Product is a superior alternative to DTT. The product is odorless, non-volatile and stable in air. Dilute solutions in air show no appreciable oxidation. Reduces organic disulfides to thiols rapidly and quantitatively in water. The reaction is reversible. Does not react with other functional groups on proteins.

syn. (2S)-2-Amino-1,4-dimercaptobutane DTBA is simply the best reducing agent for reducing disulfide bonds. Approximately 20% of human proteins are predicted to contain disulfide bonds between cysteine residues. DTBA has thiol pKa values that are approximately 1 unit lower than DTT and forms a disulfide with a similar E value.

Protein modification reagent. Used to prepare maleimide-activated proteins through EDC coupling of the carboxyl group to available protein amino groups. The product is also a probe for protein thiol groups and is non cleavable.

Cleaves tryptophan residues. The amino acid sequence of cytotoxin mitogillan was determined with peptide fragments produced by BNPS SKATOLE, Purity ca. 90%.

Spacer arm 2.8 angstroms.Protein modification reagent. Used to introduce protected thiol groups onto primary amines. The protected sulfhydryl prevents dipeptide formation. When treated with hydroxylamine a free sulfhydyl group can then be conjugated to maleimide modified protein

m.p. 42-44C°; Protective reagent for sulfhydryl groups. Quantitatively reduces disulfides. The white crystals are clear and colorless in solution. Reagent promotes proteins to unfold and maximize bonding. 99% (titration) H2O: soluble50 mg/mL