N-Hydroxysuccinimido Biotin

N-Hydroxysuccinimido Biotin (NHS-Biotin) is a widely used biotinylation reagent designed for labeling proteins, peptides, and other biomolecules through primary amine groups. Its rapid and efficient reactivity makes it an essential tool for molecular biology, biochemistry, and nanotechnology. NHS-Biotin forms stable amide bonds, enabling strong biotin-avidin interactions, which are foundational in many bioanalytical applications. This product is essential in protein detection, affinity purification, and imaging, making it a staple in research labs, pharmaceutical industries, and biotech companies. The extraordinarily high affinity between biotin and streptavidin—one of the strongest non-covalent interactions known—provides a robust and versatile platform for molecular assembly, targeted delivery, detection and biosensing, and surface functionalization across a range of scientific fields.

One of NHS-Biotin’s primary applications is in protein and peptide labeling. Its ability to target lysine residues allows for precise attachment, facilitating downstream detection via streptavidin-based assays. NHS-Biotin has been extensively used in proteomics to study protein-protein interactions, conformational changes, and membrane protein accessibility. It is also crucial in structural biology, helping researchers analyze binding sites and protein stability through biotin-streptavidin affinity methods. The reagent’s use extends to research in targeted drug delivery, where biotinylated nanoparticles enhance therapeutic precision. In imaging studies, NHS-Biotin functionalization is being explored to improve the efficiency of diagnostic tools such as biotin-labeled contrast agents for enhanced visualization.

The chemical properties of NHS-Biotin contribute to its versatility. It is highly reactive in aqueous environments, especially at physiological pH, making it ideal for modifying biomolecules under mild conditions. The reagent offers various solubility options, including Sulfo-NHS-Biotin derivatives, which enhance its compatibility in aqueous solutions. Biotin-functionalized gold nanoshells, developed using NHS-Biotin, have been explored for research in cancer imaging and therapy, demonstrating the product’s expanding role in nanomedicine. Additionally, its use in chemically cleavable biotin derivatives allows for reversible labeling, a valuable feature in transient interaction studies. The relatively small molecular size of NHS-Biotin minimizes steric hindrance, making it an effective tag that largely preserves the native function and structure of labeled biomolecules.

Industries such as biotechnology, pharmaceuticals, and materials science rely on NHS-Biotin for diverse research applications. Researchers in academia utilize it for molecular biology assays, including Western blotting, ELISA, and immunoprecipitation. In proteomics, NHS-Biotin aids in lysine residue accessibility studies, helping identify solvent-exposed regions in proteins. In the materials science sector, NHS-Biotin plays a role in surface modification, enhancing the specificity of biosensors and diagnostic tools. Biotinylation techniques employing NHS-Biotin have also contributed to advancements in cell biology by enabling targeted delivery of biotinylated molecules for imaging and functional studies.

NHS-Biotin remains a gold standard in bioconjugation chemistry, with applications spanning proteomics, drug discovery, and biomedical imaging. Its rapid reaction with primary amines, combined with biotin’s strong affinity for avidin, makes it an irreplaceable tool for researchers and scientists in academia and industry. The reagent’s expanding role in nanoparticle-based drug delivery and biosensing underscores its versatility in modern scientific research.

1. Muraoka, A., Matsuura, Y., Naitow, H., Ihara, M., & Kunishima, N. (2018). Availability of NHS biotin labeling to identify free protein lysine revealed by experiment and MD simulation. Analytical biochemistry, 557, 46-58.
2. Grumbach, I. M., & Veh, R. W. (1991). Sulpho-N-hydroxysuccinimide activated long chain biotin: a new microtitre plate assay for the determination of its stability at different pH values and its reaction rate with protein bound amino groups. Journal of immunological methods, 140(2), 205-210.