Thermo Scientific EZ-Link Maleimide-PEG2-Biotin is a medium length, maleimide Activated thiol-reactive biotinylation reagent containing 2 units of ethylene glycol in the spacer arm to improve water solubility properties.

EZ-Link Maleimide-PEG2-Biotin Features:

•Protein Label—biotinylated antibodies or other for protein methods Protein
• Thiool reactivity—reacts with sulfhydryl (-SH) groups (such as cysteine (C) side chains)
• Maleimide activation< /b>—The reaction is carried out in a buffer such as PBS at a pH of 6.5 to 7.5
• PEGylation—The spacer arm contains a hydrophilic 2-unit polyethylene glycol (PEG) ) group
• Enhanced solubility—PEGylation makes the biotinylated molecule water-soluble, helping to prevent aggregation of biotinylated antibodies stored in solution
• < b>Irreversible—Can form a permanent thioether bond; the spacer arm cannot be cleaved
• Solubility—Can be directly dissolved in aqueous buffer for labeling reaction
• < b>Medium Length—The spacer arm (total length added to the target) is 29.1 Angstroms

Maleimide-PEG2-Biotin targets antibodies, cysteine-containing peptides Simple and efficient biotinylation of other sulfhydryl-containing molecules. At pH 6.5 to 7.5, the maleimide group reacts specifically and efficiently with the reduced thiol (thiol group, -SH) to form a stable thioether bond. Hydrophilic 2 unitsPolyethylene glycol (PEG) spacer arm transfers water solubility to the biotinylated molecule, thereby reducing label stored in solution Protein aggregation. The PEG segment adds length and flexibility to the spacer arm to minimize the steric hindrance involved in binding to the avidin molecule.

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. Maleimide reagents react specifically with sulfhydryl groups (-SH) in near-neutral buffers 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.