AnaSpec Announces First Commercially Available Beta-Amyloid Peptides (1-44 to 1-49).SAN JOSE San Jose, city, United States San Jose (sănəzā`, săn hōzā`), city (1990 pop. 782,248), seat of Santa Clara co., W central Calif.; founded 1777, inc. 1850. , Calif. -- Due to challenges in synthesis due to their structure, beta-amyloid peptides with sequences 1-44 to 1-48 have not been commercially available until now. AnaSpec, a leading provider of integrated proteomics solutions, has introduced the industry's first commercially available beta-amyloid peptides for sequences 1-44, 1-45, 1-46, 1-47, 1-48 and 1-49. Amyloid Precursor Protein Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. Its primary function is not known, though it has been implicated as a regulator of synapse formation[2] and neural plasticity. , APP, is predominantly processed by a-Secretase, producing a 83-amino acid C-terminal fragment, C83; while a small amount is processed by b-Secretase, producing a 99-amino acid C-terminal fragment, C99. Subsequent cleavages of C83 and C99 by g-Secretase produce a 3-kD (p3) protein in the former and a 4-kD (beta-amyloid) protein in the latter and a CT57-59 in both fragments.1 The 4-Kd consists of beta-amyloids which are 39 to 42 amino acids in length, with beta-amyloid 1-42 being the major component of amyloid plaques which accumulate in neurons Neurons Nerve cells in the brain, brain stem, and spinal cord that connect the nervous system and the muscles. Mentioned in: Speech Disorders of Alzheimer's diseased brains.2,3 Novel cleavage sites (e and z) downstream of the g-cleavage site have recently been reported,4 which release longer beta-amyloid peptides (1-43, 1-45, 1-46 and 1-48). These longer beta-amyloid peptides have been notoriously difficult to make, due to a C-terminus sequence composed primarily of hydrophobic hydrophobic /hy·dro·pho·bic/ (-fo´bik) 1. pertaining to hydrophobia (rabies). 2. not readily absorbing water, or being adversely affected by water. 3. amino acids. The successful synthesis and commercialization of these longer beta-amyloid peptides represents a significant achievement on the part of AnaSpec. AnaSpec president, Dr. Anita Hong, noted, "Drawing on our many years of peptide synthesis In organic chemistry, peptide synthesis is the creation of peptides, which are organic compounds in which multiple amino acids bind via peptide bonds which are also known as amide bonds. experience, AnaSpec is committed to supporting the research efforts of our customers with the most innovative tools we can develop. With the successful commercialization of these longer beta-amyloid peptides, we are pleased to offer an even broader selection of amyloid-related products for our customers." Company Info AnaSpec, Inc. is a leading provider of integrated proteomics solutions to pharmaceutical, biotech, and academic research institutions throughout the world. With a vision for innovation through synergy, AnaSpec focuses on three core technologies: peptides, detection reagents (dyes, assay kits, & antibodies), and combinatorial chemistry Combinatorial chemistry involves the rapid synthesis or the computer simulation of a large number of different but structurally related molecules. Introduction Synthesis of molecules in a combinatorial fashion can quickly lead to large numbers of molecules. . Established in 1993, AnaSpec's ISO (1) See ISO speed. (2) (International Organization for Standardization, Geneva, Switzerland, www.iso.ch) An organization that sets international standards, founded in 1946. The U.S. member body is ANSI. 9001:2000 certified headquarters and manufacturing facilities are located in San Jose, CA. 1. Selkoe DJ. Nature 399: A23 (1999). 2. Suzuki, N., et al. Science 264, 1336 (1994). 3. Iwatsubo, T. et al. Neuron neuron, specialized cell in animals that, as a unit of the nervous system, carries information by receiving and transmitting electrical impulses. neuron or nerve cell Any of the cells of the nervous system. 13, 45 (1994). 4. Qi-Takahara, Y. et al. J. Neurosci. 25, 436 (2005). |
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