SANTA CLARA, Calif. – Affymetrix, Inc. (NASDAQ:AFFX) today launched its Anatrace(R) brand Neopentyl Glycol (NG) Class(TM) Detergents, the next generation of detergents to significantly advance the study of integral membrane proteins (IMPs), the most important proteins found in the human genome.

Developed by leading chemists, and available only from Affymetrix, the NG Class represents a new family of detergents based on the maltose-neopentyl amphiphile design first described in a study recently published in the journal Nature Methods1. The new NG Class was found to be more capable than current leading detergents, such as n-dodecyl-B-D-maltoside (DDM), in promoting crystallization of IMPs in preparation for structural and functional studies.

“We are excited to make this breakthrough available to life scientists who are intrigued by the mystery of these essential and pervasive proteins,” said Andy Last, Chief Commercial Officer at Affymetrix. “Our new NG Class Detergents give biologists enhanced tools to solve the structure of membrane proteins using advanced techniques, such as nuclear magnetic resonance and X-ray diffraction.”

Membrane proteins are important because they mediate the transfer of materials and signals between cells and their environment, and they account for a large portion of the human genome’s coding region. Moreover, they are the target of 50 percent of current pharmaceutical agents. Using most conventional detergents, IMPs can be successfully extracted. However, due to the hydrophobic nature of membrane proteins, they tend not to stabilize and become denatured and/or aggregated after extraction. If IMPs are not stabilized enough to crystallize, then they cannot be effectively studied, nor fully understood.

In the December 2010 Nature Methods study, researchers extensively compared the performance of new NG Class Detergents to existing popular amphiphiles in several areas, including extraction, stabilization, and crystallization. The study demonstrated a “superior” performance in each of these categories and concluded that “representatives of this maltose-neopentyl glycol amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems leading to enhanced structural stability and successful crystallization” (Nature Methods, 2010).

Because membrane proteins have diverse sequences, shapes, and properties, Affymetrix is launching a suite of three Anatrace brand NG Class Detergents as substitutes for the three most popular glucoside detergents, lauryl and decyl maltosides and octyl glucoside.

About Affymetrix

Affymetrix technology is used by the world’s top pharmaceutical, diagnostic, and biotechnology companies, as well as leading academic, government, and nonprofit research institutes. More than 2,000 systems have been shipped around the world and more than 23,000 peer-reviewed papers have been published using the technology.

Affymetrix is headquartered in Santa Clara, Calif., and has manufacturing facilities in Santa Clara, Cleveland, Ohio, and Singapore. The company has about 1,000 employees worldwide and maintains sales and distribution operations across Europe and Asia. For more information about Affymetrix, please visit http://www.affymetrix.com.

Forward-looking statements

All statements in this press release that are not historical are “forward-looking statements” within the meaning of Section 21E of the Securities Exchange Act as amended, including statements regarding Affymetrix’ “expectations,” “beliefs,” “hopes,” “intentions,” “strategies” or the like. Such statements are subject to risks and uncertainties that could cause actual results to differ materially for Affymetrix from those projected. These and other risk factors are discussed in Affymetrix’ Form 10-K for the year ended December 31, 2009, and other SEC reports for subsequent quarterly periods.

NOTE: Affymetrix, the Affymetrix logo, Anatrace, and NG Class are trademarks or registered trademarks of Affymetrix Inc.

1 Chae, P. S., et al. Maltose-Neopentyl Glycol (MNG) Amphiphiles for Solubilization, Stabilization and Crystallization of Membrane Proteins. Nature Methods7(12)1003-1008 (2010).