N-Hydroxysuccinimide TCI H0623

TCI H0623 N-Hydroxysuccinimide, commonly abbreviated as NHS, is a carboxyl-activating reagent that forms the backbone of modern peptide chemistry and bioconjugation. When paired with a carbodiimide such as EDC or DCC, NHS converts carboxylic acids into NHS esters that are considerably more reactive toward primary amines. These active esters then form amide bonds efficiently with the amino groups of lysine residues on proteins, with amine groups on linkers, or with the next amino acid in a peptide synthesis sequence, which is why this reagent is almost always kept on hand in biochemistry laboratories.

The property that makes NHS so dependable is its ability to suppress side reactions while simultaneously improving coupling yields. Without NHS, the O-acylisourea intermediate generated from a carbodiimide readily rearranges into unreactive N-acylurea or is wastefully hydrolysed; the presence of NHS traps that intermediate as an active ester that is far more stable and remains selective toward amines. NHS also helps suppress racemisation during peptide synthesis, an important advantage whenever stereochemical purity is a requirement. It takes the form of a white crystalline solid that dissolves in water and in polar organic solvents.

In Indonesian laboratories, NHS is a routine item in university biochemistry groups, research institutes, and industrial R&D units engaged in peptide synthesis, protein labelling, and the preparation of conjugated reagents. Because it is used in small portions across many separate couplings, a single container typically supports an extended series of experiments. Its stability as a crystalline solid also makes it practical for facilities where reagents are ordered periodically rather than continuously, provided humidity is properly controlled.

• Peptide bond formation in solution-phase and solid-phase synthesis, where NHS esters couple amino acid building blocks efficiently while suppressing the racemisation that would compromise stereochemical purity of the final peptide.
• Protein bioconjugation via lysine residues, where NHS activation of carboxyl-bearing labels allows stable amide linkage to primary amine groups on the protein surface under mild aqueous conditions.
• Carbodiimide-mediated coupling with EDC or DCC, in which NHS intercepts the unstable O-acylisourea intermediate and converts it into a longer-lived active ester, markedly raising coupling efficiency.
• Preparation of crosslinkers and linker reagents, where NHS-activated termini are introduced onto spacer molecules so that the resulting reagent reacts selectively with amine functionalities during later assembly steps.
• Surface functionalisation of amine-bearing supports and resins, where NHS ester chemistry immobilises carboxyl-containing molecules through covalent amide bonds that resist hydrolysis better than physically adsorbed alternatives.

• Solubility: soluble in water and polar organic solvents

Store N-Hydroxysuccinimide in a tightly closed original container in a cool, dry place away from moisture, since the solid is hygroscopic in practice and water uptake degrades activation performance. Keep the container closed when not in use and allow it to reach room temperature before opening if it has been stored cold, so that condensation does not form on the crystals. Handle the material in a fume hood or a well-ventilated area, wearing gloves, safety glasses, and a laboratory coat, and avoid generating or inhaling dust during weighing. Prepare activated ester solutions fresh where the protocol calls for it, as NHS esters hydrolyse in aqueous media over time. Consult the manufacturer's safety data sheet before first use and follow local institutional rules for chemical waste disposal.

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