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ProSep® Ultra Plus Chromatography Media

Designed for high throughput affinity purification of monoclonal antibodies and other proteins.



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Reference overviewApplication
Determining the Useful Lifetime of Chromatography Resins: Prospective Small-Scale Studies
O’Leary et al.,Biopharm, September 2001, pp 10 -18
Biopharm, September 2001, pp 10 -18  2001

Pressure-flow relationships for packed beds of compressible chromatography media at laboratory and production scale
Stickel J.J.; Fotopoulos A.
Biotechnology Progress, 17/4 (744-751), 2001  2001

Process development studies
Determining the useful lifetime chromatography resins: Prospective small-scale studies
O'Leary R.M.; Feuerhelm D.; Peers D.; Xu Y.; Blank G.S.
BioPharm ( BIOPHARM ) (United States) 2001, 14/9 (10-18)  2001

Process development studies
Affinity chromatography is vital to protein research and development

Process development studies
Industrial purification of pharmaceutical antibodies: development, operation, and validation of chromatography processes.
Fahrner RL, Knudsen HL, Basey CD, Galan W, Feuerhelm D, Vanderlaan M, Blank GS.
Biotechnol Genet Eng Rev 2001;18:301-27  2001

Process development studies
Preparative Immunoaffinity Techniques
Michael Price and Kami Beyzavi; Peptide Antigens, A Practical Approach, Chapter 5
Peptide Antigens, A Practical Approach, Chapter 5  1999

Performance comparison of Protein A affinity chromatography adsorbents for purifying recombinant monoclonal antibodies
Robert L Fahrner, Duncan H Whitney, Martin Vanderlaan, Gregory S Blank.
Biotechnol. Appl. Biochem, Vol 30 121-128, 1999  1999

Performance comparison of Protein A affinity-chromatography sorbents for purifying recombinant monoclonal antibodies
Fahrner, et al.,Biotechnol. Appl. Biochem. (1999) 30, 121-128
Biotechnol. Appl. Biochem. (1999) 30, 121-128  1999

The optimal flow rate and column length for maximum production rate of Protein A affinity chromatography
R.L Fahrner, H.V. Iyer, G.S. Blank
Bioprocess Engineering 21 (1999) 287-292 - Springer-Verlag.  1999

Process development studies
Development, validation and application of an ultra-sensitive two-site enzyme immunoassay for human follistatin
LW Evans, S Muttukrishna and NP Groome
Journal of Endocrinology, 156, 275-282, 1998  1998


What is the difference between ProSep-vA Ultra and ProSep-vA High Capacity chromatography media?Prosep-vA Ultra uses a 700 angstrom pore size porous glass and ProSep vA High Capacity uses a 1000 Angstrom porous glass. The Prosep-vA Ultra has a greater surface area due to the smaller pore size, which allows the immobilization of a larger amount of protein A. The increased amount of protein A results in a higher capacity resin.
How do I choose between ProSep-vA Ultra versus ProSep-vA High Capacity?Prosep-vA Ultra has a higher binding capacity than ProSep-vA High Capacity - ≥ 56mg/ml vs ≥ 40 mg/ml.

ProSep-vA High Capacity has a larger pore size and may perform better when purifying fusion proteins or antibody conjugates with molecular weights above 150 kD.
What is the shelf life of the Prosep-A family of protein A affinity media?One Year. Shelf life studies are ongoing and will be increased as data becomes available. Please contact Technical Service for further shelf life information.
What is Prosep-vA ?ProSep-vA is native protein A derived from Staphylococcus aureus which has been immobilized onto porous glass beads. ProSep-vA is available on glass of two diffferent porosities - ProSep-vA ultra (700 angstroms) and ProSep-vA High Capacity (1000 angstroms)
Do you provide reguatory support?A regulatory reference document is available for ProSep-vA High Capacity and will soon be available for Prosep-vA Ultra.

As the raw materials and the chemistry used in the manufacture of ProSep-vA Ultra are the same as for ProSep-vA High Capacity , the regulators will be familiar with the product. ProSep-vA High Capacity has been and is widely used in various licensed MAb products and products in clinical trails.

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Biopharmaceutical Manufacturing > Downstream Processing > Chromatography > Affinity Chromatography