Thermo Scientific SulfoLink Coupling Resin is porous, crosslinked, 6% beaded agarose that has been activated with iodoacetyl groups for covalent immobilization of cysteine-peptides and other sulfhydryl molecules.
Features of SulfoLink Coupling Resin:
• Specific to sulfhydryl (-SH) groups—iodoacetyl groups react specifically with sulhydryls to form irreversible thioether bonds • Fast—spin columns increase protocol speed; prepare and couple samples in 2 hours (peptides) to 3.5 hours (proteins) • Flexible coupling conditions—use pH 7.5 to 9.0 aqueous buffers, organic solvent (e.g., 20% DMSO) or denaturant (guanidine·HCl), as needed for protein or peptide solubility during coupling reaction • Easy-to-follow instructions—streamlined protocols for sample preparation, immobilization, and affinity purification • High capacity—Immobilize 1 to 2 mg of peptide or 2 to 20 mg of protein per 2 mL column of SulfoLink Coupling Resin
When incubated with a solution of peptide or protein that contains reduced cysteine residues, the iodoacetyl groups of SulfoLink Resin react specifically and efficiently with the exposed sulfhydryls (-SH) to form covalent and irreversible thioether bonds that permanently attach the peptide or protein to the resin. The result is a custom-made affinity resin for purification of antibodies, antigens and other molecules of interest. Choose one of two convenient SulfoLink Immobilization Kits for peptides or proteins. Each kit contains all the reagents for preparing the sample and five columns containing 2 mL of SulfoLink Resin that can be used in either gravity-flow or centrifuge format for efficient coupling reactions and multiple cycles of affinity purification. A single-column Trial Kit for use with either peptides or proteins is also available, or the SulfoLink Coupling Resin can be purchased separately.
Applications: • Immobilize peptides having terminal cysteine residues to purify antibodies that were generated against peptide immunogens prepared by maleimide conjugation • Immobilize antibodies in oriented manner through hinge-region sulfhydryls to ensure that antigen binding sites are not sterically hindered for antigen affinity purification