Athena Environmental Sciences, Inc. Receives A Phase-I SBIR Grant To Develop A Protein Expression and Purification Instrument

Baltimore, Maryland, September 26th, 2009-- Athena Enzyme Systems™, a division of Athena Environmental Sciences, Inc., provides products and services that help researchers and manufacturers improve the production and recovery of recombinant proteins. The company has recently been awarded a NSF Phase I SBIR grant to design and build a bench-top protein expression and purification instrument based on its licensed YebF technology.

Athena Enzyme Systems™ (AthenaES®) is based in Baltimore, Maryland and specializes in the development and commercialization of advanced biotechnology-based products and provides life cycle contract R&D and manufacturing services for development of innovative ideas from conceptualization to production of product. It manufactures and sells products which include: Expression Media- a proprietary line of bacteriological media specifically designed to increase the expression of recombinant proteins; BRFF Brand™ cell culture reagents- a line of serum-free media for culturing human cell lines along with accessory products for cell culture; PDQ Protease Assay™ - a broad-spectrum, one step protease assay; Athena Enzymes™- specialty biocatalysts for research, environmental and specialty chemical applications; Protein Refolding Kit- a screening tool for identifying suitable conditions for refolding denatured proteins; ACES™ Expression Kits- three different protein expression modalities in three different kits to help researchers express and purify recalcitrant recombinant proteins.

AthenaES® was awarded a Phase-I SBIR grant with a start date of July 1 by the National Science Foundation (NSF). This Small Business Innovation Research (SBIR) program grant is entitled: Fully Integrated Seamless Protein Production and Purification System. The focus of the grant is to develop a completely automated bench-top instrument that will integrate upstream production (i.e., biomass production and recombinant protein induction) with downstream purification (i.e., protein capture and specification-level purification of final product). The technology driving the seamless integration of the upstream and downstream processes is the YebF-based secretory expression system. One of the three ACES™ Expression Kits utilizes this (exclusively) licensed technology which facilitates the expression and recovery of many difficult-to-purify recombinant proteins.

AthenaES®’ motto- “simple solutions for complex proteins” -embodies the company’s philosophy of providing reliable solutions to protein production needs. The scientific staff strives to make products of the highest quality and backs their performance with real-world applications testing. Staff scientists will gladly provide help and support to researchers having difficulties expressing a target recombinant protein. AthenaES®’ expression products have been in use by scientists in commercial, governmental and academic settings for over 10 years. The company also provides life-cycle contract research to commercial, governmental and academic clients who require the production and purification of recombinant and native proteins, as well as providing custom medium manufacturing to those researchers who need specialized “omission” media.

A contract protein production project typically begins with several experiments designed to maximize the expression of the target recombinant protein. Optimizing a protein expression campaign invariably results in increased final product yields. Staff scientists are available to guide customers through the development process, if need be.

AthenaES® supplies researchers who routinely conduct labeling experiments with custom omission medium. The company has worked with the SILAC (Stable Isotope Labeling with Amino acids in Cell culture) community for several years now providing its researchers with customer-specific cell culture media in support of their labeling or other experiments that require a mammalian tissue culture medium without certain raw material components (e.g., without L-arginine or L-lysine).

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