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Enzo Life Sciences Introduces Rapid Forced Degradation Analysis Kit

May 2010

Enzo Life Sciences has introduced a new assay which provides an improved thermal shift approach for assessment of protein stability through monitoring protein aggregation, rather than protein unfolding.
Forced degradation studies involve exposing a protein to harsher conditions than the pharmaceutical product would normally experience and determining at what point it degrades. ProteoStat™ Thermal Shift Stability Assay provides a rapid high-throughput fluorescence-based approach for assessing a range of parameters impacting the stability of monoclonal antibodies and recombinant therapeutic proteins, based upon their exposure to systematically increasing thermal stress, under a variety of solution conditions. This procedure is based upon the expectation that proteins degraded in this manner reflect the degradation pathway(s) experienced during a product's lifetime. The assay can be performed using either a conventional fluorimeter equipped with heating control or a real-time PCR instrument.
The thermal shift assay facilitates understanding of the underlying mechanisms impacting protein stability, as well as predicting the stability of therapeutic proteins upon long-term storage, screening the relative stability of protein variants (e.g. amino acid substitution/deletion mutants, PEGylated proteins) and providing other critical information pertaining to the development of optimal protein formulations.

The ProteoStat™ Thermal Shift Stability Assay kit includes a fluorescent dye which detects protein aggregation arising from thermally-induced protein structural destabilization. From the thermal shift assay, a temperature at which the bulk of the protein becomes aggregated can readily be identified.
“Aggregation temperature is an indicator of protein stability and can be used to optimize conditions that enhance protein stability as well as identify ligands that bind and confer structural stability to a protein of interest. Conditions that increase the aggregation temperature increase the stability of the protein.” stated Wayne Patton, Ph.D., Chief Scientific Officer for Enzo Life Sciences. “This assay has broad applicability in bioprocessing and pharmaceutical manufacturing industry” he continued. The new assay facilitates understanding of the underlying mechanisms impacting protein stability, and because it is not dependent upon measuring exposed hydrophobic regions arising from protein unfolding, is tolerant of detergents, micelle formation and certain ligands and proteins possessing hydrophobic characteristics.

More information on these products is available on-line at their website:, or to receive more technical product information, e-mail, phone 610-941-0430, or write Enzo Life Sciences, Inc. at 5120 Butler Pike, Plymouth, PA 19462 USA.

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