for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
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Storage & shipping
Store at -20°C,Desiccated Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
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Quality documents
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
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Literature proof
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Overview
Product introduction:
Sulfo-NHS-LC-Desthiobiotin is a long-chain, amine-reactive labeling reagent whose biotin-like group is elutable from streptavidin, making it ideal for purified or cell surface protein labeling and purification.
Features of EZ-Link Sulfo-NHS-LC-Desthiobiotin:
• Desthiobiotin—analog of biotin allows easy elution from streptavidin, an ideal feature for affinity purification applications • Protein labeling—tag antibodies or proteins in purified or mixed samples to enable high recovery in pull-down assays with streptavidin beads • Cell surface labeling—modifies only surface proteins of whole cells because the negatively charged reagent does not permeate cell membranes • Amine-reactive—reacts with primary amines (-NH2), such as lysine side-chains, or the amino-termini of polypeptides • Soluble—charged sulfo-NHS group increases reagent water solubility compared to ordinary NHS-ester compounds
Sulfo-NHS-LC-Desthiobiotin is a variant of biotin that is activated as a sulfo-NHS ester with a long-chain (LC) spacer arm to covalently label primary amines (-NH2) of proteins or other molecules with desthiobiotin groups. The desthiobiotin tag binds to streptavidin and other biotin-binding proteins with high specificity yet readily elutes with mild conditions (i.e., by competitive displacement with regular, free biotin). As such, this reagent is a useful alternative toDesthiobiotin is a single-ring, sulfur-free analog of biotin that binds to streptavidin with nearly equal specificity but less affinity than biotin (1/Kd = 1011 vs. 1015 M, respectively). Consequently, desthiobiotinylated bait proteins and their interacting partners can be eluted readily and specifically from streptavidin affinity resin using mild conditions based on competitive displacement with free biotin. For pull-down assay experiments with biological samples, this soft-release characteristic of desthiobiotin also helps to minimize co-purification of endogenous biotinylated molecules, which remain bound to streptavidin upon elution of the target protein complexes with free biotin. The modified avidin-biotin affinity system also eliminates the need to use harsh elution conditions that might disassociate complexes and/or damage the target protein or cell. Desthiobiotin-based techniques are ideal when using native or recombinant proteins that are not expressed with a fusion tag and when isolating captured proteins under native conditions, such as targeting intact cells or cell surface proteins.
Labeling with NHS Ester Reagents N-Hydroxysulfosuccinimide (NHS) esters of biotin are the most popular type of biotinylation reagent. NHS-activated biotins react efficiently with primary amino groups (-NH2) in alkaline buffers to form stable amide bonds. Proteins typically have several primary amines that are available as targets for labeling, including the side chain of lysine (K) residues and the N-terminus of each polypeptide. Most sulfo-NHS esters are directly water soluble but not membrane permeable. Plain NHS esters are less soluble in aqueous buffers but are membrane permeable.
• Spacer:Short, 17.3 Å
• Labeling Method:Chemical Labeling
• Cell Permeability::Cell-Impermeant
Specifications
Storage
Store at -20°C, Desiccated
Shipped In
Ice chest + Ice pads
This product requires cold chain shipping. Ground and other economy services are not available.
Product Properties
Reactivity
Amine
Documentation
📋 Safety Data Sheet (SDS)
Comprehensive hazard, handling, storage, and regulatory compliance document.
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