Press Release

X-BODY Biosciences Launches Platform for Rapid Discovery of Human Antibody Therapeutics With Presentations at the 21st Annual IBC Antibody Engineering Conference

WALTHAM, Mass., Nov. 30, 2010 /PRNewswire/ -- X-BODY Biosciences, a developer of monoclonal antibody therapeutics, today announced the launch of its Protein Chain Reaction(TM) antibody discovery platform. The company will give its first public presentations at IBC's 21st Annual International Conference on Antibody Engineering held December 5-9th in San Diego. Richard Wagner, Ph.D., Co-Founder and Executive Chairman of X-BODY will present a talk entitled, "Discovery and Characterization of hMAB Targeting an RTK Implicated in Metastasis by Live Cell Screening and Interrogation of Fully Human Libraries with Deep Sequencing" on Monday, December 6th at 11:00AM. Yan Chen, M.D./Ph.D., VP of Antibody Research at X-BODY will present a poster entitled, "Rapid Generation of hMABs Using a Novel Integrated Platform" at the conference.

X-BODY's fully human library captures the natural antibody repertoire. Compared to synthetic libraries, fully human libraries reduce the probability of side effects due to immune responses. The platform's Protein Chain Reaction(TM) allows for screening against cell surface targets in their native state on live cells or purified target proteins. X-BODY's platform employs the high throughput SRU BIND® protein detection system to screen for high affinity antibodies. X-BODY, in collaboration with SRU Biosystems, has validated a novel BIND® Biosensor design for use with the commercially available SRU BIND® Reader that results in a >500-fold increase in sensitivity over SRU’s previous sensor technology. The novel biosensor allows for measurement of sub-nanomolar affinity interactions in an automated 384-well or 1536-well microplate format.

X-BODY's versatile Protein Chain Reaction(TM) screening system with deep sequencing of thousands of hits allows for the rapid identification of high quality leads with the following therapeutically relevant properties:

• High affinity
• High selectivity
• Species cross-reactivity
• Broad epitope coverage
• Low immunogenicity

• High affinity soluble VH domain binders
• "Bio-Better" follow-on hMABs
• Optimized VL pairs
• Multimeric VH binders
• Bispecific antibodies