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Past Events

 

 

March 15-19, 2009

 

6th HIC/RPC Bioseparation Conference

Silverado Resort Napa, CA

Conference website: http://www.hic-rpc.org/


Poster Session: Monday March 16 - 4:15 - 5:30 pm:

 

 

Authors:

J. Fisher, R. Agarwal and M. Kinzey

 

Abstract:

 

For over 20 years, Amberchrom™ reversed phase resins have been used for production-scale purification of biotherapeutics. Most of these processes involve the use of hazardous solvents for the reversed phase purification of peptides and oligonucleotides. However, Amberchrom™ CG71 has unique properties that allow it to be used in a gentler hydrophobic interaction mode for protein purification. Additionally, the use of nonflammable solvents such as hexylene glycol, give greater flexibility in manufacturing. Lastly, Amberchrom CG71 works well for the selective removal of detergents and color bodies from recombinant protein feedstreams. In this study we demonstrate the use of Amberchrom™ CG71M, an acrylic 75 micron resin, for protein purification with a variety of different conditions.

 

Presenter bio:

Jon Fisher has over 15 years of experience in the life sciences purification market. Jon obtained his undergraduate degree in toxicology at The University of the Sciences in Philadelphia and his MBA at Temple University. He is currently the Advanced Biosciences Technical Service Manager for the Americas at Rohm and Haas Company. His responsibilities include oversight of applications development for Advanced Bioscience products, as well as overall technical support for these products in the Americas.

 

 

 

 

May 17-20, 2009

 

TIDES
Oligonucleotide and Peptide Technology and Product Development

Red Rock Casino, Resort and Spa, Las Vegas, NV

Booth # 102

Conference website: http://www.ibclifesciences.com/tides/overview.xml

 

Poster Session


 

Authors:

J. Fisher and M. Kinzey

 

Abstract:

 

There are currently over 60 marketed peptide drugs and this market is projected to grow at double-digit rates during the next 5 to 10 years. At the same time, newer peptides tend to be larger and therefore more complex than their older counterparts. This increase in demand and molecule complexity fuels the need for better synthesis and purification strategies. Rohm and Haas has recently introduced several new polymeric cation exchange resins for the capture and purification of synthetic, natural, and recombinant peptides, that are tailored to accommodate the increasing demands of peptide manufacturing processes. Amberlite™ FPC 3500 resin is an acrylic weak-acid cation exchange resin, and Amberlite™ FPX62 resin is a polystyrenic strong-acid cation exchange resin. These products have been designed to provide economical capture and purification of small MW biologicals. In this paper we present general properties of the resins, and demonstrate their use for the purification of several peptides

 

 

 

July 19-22, 2009


22nd Preparative and Process Chromatography Symposium
Loew's Hotel, Philadelphia, PA
Conference website: http://faculty.virginia.edu/PREP2009/doc/HomePage.html

 

 

Poster Session


 

Authors:

J. Fisher and M. Kinzey

 

Abstract:

 

There are currently over 60 marketed peptide drugs and this market is projected to grow at double-digit rates during the next 5 to 10 years. At the same time, newer peptides tend to be larger and therefore more complex than their older counterparts. This increase in demand and molecule complexity fuels the need for better synthesis and purification strategies. Rohm and Haas has recently introduced several new polymeric cation exchange resins for the capture and purification of synthetic, natural, and recombinant peptides, that are tailored to accommodate the increasing demands of peptide manufacturing processes. Amberlite™ FPC 3500 resin is an acrylic weak-acid cation exchange resin, and Amberlite™ FPX62 resin is a polystyrenic strong-acid cation exchange resin. These products have been designed to provide economical capture and purification of small MW biologicals. In this paper we present general properties of the resins, and demonstrate their use for the purification of several peptides