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San Jose, CA, United States, 2006/09/05 - AnaSpec, Inc. is a leading provider of integrated proteomics solutions for worldwide life science research. With a vision for innovation through synergy, and expertise in three primary technologies: peptides, detection reagents, & combinatorial chemistry..
AnaSpec carries a broad product line of biochemicals and reagents for basic research, high-throughput screening and drug discovery. In conjunction, AnaSpec provides premier custom services including peptide synthesis, antibody production, and assay development. AnaSpec holds a California Drug Manufacturing License (License #41747) and a FDA Registration for GMP Drug Manufacturing (Registration #2951078).
Caspases are a family of cysteine-dependent aspartate specific proteases involved in the destruction of cells. In a normal, healthy human being, damaged or mutated cells are regularly destroyed to protect the rest of the body. The induction of caspase-dependent programmed cell death triggers a tightly-controlled cascade of events with the initiator caspases activating effector caspases. These effector caspases not only activate other effector caspases and provide feedback to initiator caspases, they also cleave cellular substrates resulting in morphological changes such as DNA fragmentation, membrane blebbing or apoptotic body formation. These changes, characteristics of apoptosis, ultimately lead to the death of a cell. Caspases, however, may not be the only enzymes involved in cell death; cell death may still occur even if all caspases are all blocked (Reviewed in 1).
Because of their important role in apoptosis and cell signaling, and their identification as drug-screening targets, there is a recognized need for a wide range of caspase substrates and inhibitors. As a leading provider of premium quality peptides and detection reagents, AnaSpec has introduced an extensive list of caspase substrates (including both chromogenic and fluorogenic variations) and caspase inhibitors.
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1. Thornberry, NA. and Y. Lazebnik, Science 281, 1312-1316 (1998).