Thiophilic Separopore® (Agarose) 4B-CL

Applications: Thiophilic affinity purification is based on the ability of some proteins, particularly immunoglobulins, to bind to this immobilized ligand. The term "Thiophilic" refers to an affinity for sulfone groups that lie in close proximity to thioether groups. Thiophilic adsorption is promoted by water-structuring salts. It has been suggested that the interaction of IgY and ligand results from combined electron donating and accepting action of the ligand or, alternatively, a mixed mode hydrophilic-hydrophobic interaction.

Thiophilic Separopore 4B-CL is useful in purification of proteins, especially immunoglobulin G. Thiophilic Separopore 4B-CL allows purification of immunoglobulins from all animal species under mild conditions (pH 8.0, low salt concentration, elution at physiological pH).

Technical specifications:

• Active group: 2-Mercaptopyridine
• Matrix: Separopore 4B-CL (highly crosslinked agarose, 4%)
• Particle size range: 52 - 165 μm
• Matrix activation: Divinyl sulfone
• Matrix attachment: Thiol
• Matrix spacer: 5 atoms
• Active group density: 3 mg / ml drained gel
• Binding capacity: 30 - 45 mg human IgG / ml drained gel
• pH stability: 3 - 11 (long term), 2 - 13 (cleaning)
• Storage: 4 - 8 C

References:

• Purification of the 90 kDa heat shock protein (hsp90) and simultaneous purification of hsp70/hsc70,hsp90 and hsp96 from mammalian tissues and cells using thiophilic interaction chromatography. Biomed Chromatogr. (2009) 23: 1208-16.
• Thiophilic interaction chromatography (TIC) of amyloid-beta protein precursor. J Alzheimers Dis. (2007) 12: 143-9.
• Optimization of a mouse recombinant antibody fragment for efficient production from Escherichia coli. Protein Expr Purif. (2007) 52: 219-29.
• Novel hydrophobic interaction chromatography matrix for specific isolation and simple elution of immunoglobulins (A, G, and M) from porcine serum. J Chromatogr A. (2006) 1122: 28-34.
• Fractionation and purification of the enzymes stored in the latex of Carica papaya. J Chromatogr B Analyt Technol Biomed Life Sci. (2003) 790: 229-38.
• A simplified procedure for the isolation of immunoglobulins from human serum using a novel type of thiophilic gel at low salt concentration. J Immunol Methods. (1998) 219: 109-18.
• Salt-independent binding of antibodies from human serum to thiophilic heterocyclic ligands. J Chromatogr B Biomed Sci Appl. (1998) 709: 189-96.
• Comparison of the protein adsorption selectivity of salt-promoted agarose-based adsorbents. Hydrophobic, thiophilic and electron donor-acceptor adsorbents. J Chromatogr A. (1998) 800: 151-9.
• Separation of monoclonal antibodies from cell-culture supernatants and ascites fluid using thiophilic agarose. Mol Biotechnol. (1997) 8: 279-81.
• Ligand structure of the divinylsulfone-based T-gel. J Chromatogr A. (1997) 787: 47-54.
• Purification of murine IgG1 on group specific affinity sorbents. Bioseparation. (1996) 6: 165-84.
• Purification of monoclonal antibodies to Le(y) and Le(d) carbohydrate antigens by ion-exchange and thiophilic-adsorption chromatography. Bioseparation. (1995) 5: 141-6.
• Behaviour of human immunoglobulin G subclasses on thiophilic gels: comparison with hydrophobic interaction chromatography. J Chromatogr. (1993) 616: 197-204.
• Selective adsorption of immunoglobulins and glucosylated proteins on phenylboronate-agarose. J Chromatogr. (1992) 604: 109-15.
• Thiophilic adsorbents for RIA and ELISA procedures. J Immunol Methods. (1991) 143: 143-9.
• Cascade-mode multiaffinity chromatography. Fractionation of human serum proteins. J Chromatogr. (1991) 550: 751-64.
• Protein chromatography with pyridine- and alkyl-thioether-based agarose adsorbents. J Chromatogr. (1990) 499: 235-47.
• Covalent chromatography and salt-promoted thiophilic adsorption. Anal Biochem. (1989) 176: 330-7.
• Thiophilic adsorption: a comparison of model protein behavior. Biochemistry. (1987) 26: 7199-204.
• A one-step purification method for monoclonal antibodies based on salt-promoted adsorption chromatography on a 'thiophilic' adsorbent. J Immunol Methods. (1987) 102: 173-82.

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