Thermo Scientific™ SulfoLink™ Coupling Resin

Description

Thermo Scientific™ SulfoLink Coupling Resin is iodoacetyl-activated for the covalent immobilization of sulfhydryl-containing peptides or proteins for affinity purification.

Complete SulfoLink Immobilization Kits are available for peptides and proteins. Each kit contains all the reagents for preparing the respective peptide or protein sample and five columns containing 2mL 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.

Highlights:

• Specific conjugation through sulfhydryl (-SH) groups – the iodoacetyl groups react specifically with sulhydryls to form irreversible thioether bonds

• Separate kits optimized for peptides or proteins – kits include optimized reagents for preparing peptide or protein samples for efficient immobilization

• 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 2mg peptide or 2 to 20mg protein per 2mL column of SulfoLink Coupling Resin

Includes:

Kits contain SulfoLink Resin Columns (2mL), protein or peptide preparation reagents (e.g., reducing agent), coupling buffer, wash solution, L-cysteine solution (for quenching) and desalting columns (protein kit only)

Recommended for:

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