Thermo Scientific EZ-Link Iodoacetate-LC-Biotin is a medium-length, haloacetyl-activated thiol-reactive biotin Phytogenating reagent that forms stable irreversible thioether bonds at alkaline pH.

EZ-Link Iodoacetyl-LC-Biotin Features:

•Protein Labeling—biotinylated antibodies or other proteins for protein methods
• Membrane permeability—Can be used for intracellular (intracellular) labeling
• Thiool reactivity—With sulfhydryl (-SH) groups (e.g., cysteine amino acid (C) side chain) reaction
• Iodoacetic acid activation—Reaction in Tris or borate buffer at 7.5 to 8.5 pH in the dark
• < b>Irreversible—Can form permanent thioether bonds; cannot cleave spacer arm
• Solubility—Must be dissolved in DMSO or DMF and then further diluted in aqueous buffer
br>•Medium Length—The spacer arm (total length added to target) is 27.1 angstroms; contains hexamethylenediamine extension

Iodoacetyl-LC-Biotin is a haloacetyl-biotin A compound used to label protein cysteine and other molecules containing sulfhydryl groups. This reagent reacts specifically with reduced thiols (-SH) in alkaline buffers to form permanent (irreversible) thioether bonds. The unique feature of iodoacetyl-LC-biotin is its extended and chemically simple hexamethylenediamine spacer arm.

We manufacture biotin reagents to ensure the highest possible level of overall product integrity, consistency and performance for intended research applications.

Biotinylation reagents vary in reactivity, length, solubility, cell permeability, and cleavability. Three types of Sulfhydryl-reactive compounds Available: maleimide, iodoacetyl and pyridyldisulfide. Iodoacetyl reagent reacts specifically with sulfhydryl groups (-SH) at pH 8.3 to form permanent thioether bonds.

In proteins, sulfhydryl groups are found where cysteine (C) residues are present. The cystine disulfide bond must be reduced in order to obtain a sulfhydryl group that can be labeled. The disulfide bonds in the hinge region of antibodies can be selectively reduced to form functional half-antibodies that can be labeled.

Applications:
• Electron microscopy studies of protein spatial relationships (Ref. 1)
• Use of avidin-biotin complexes under electron microscopy Localizing SH1 thiols in the myosin head (Ref. 2)