A 14 aa peptide corresponding to the known b-secretase site of human APP590-603 were synthesized and purified by HPLC. beta-amyloid (Abeta) deposition in the brain is the hallmark of Alzheimer's Disease (AD). To initiate Ab formation, beta-secretase cleaves APP at the N-terminus of Ab to release APPsb (~100kD soluble NT-fragment), and C99, a 12-kD CT membrane fragment. Alternatively, alpha-secretase cleaves within the Ab to prevent the formation of Ab. Cleavage by a-secretase produces a soluble N-terminal fragment, APPsa, and a 10-kD membrane C-terminal fragment, C83. Both C99 and C83 can be further cleaved by gamma-secretase releasing Ab and a nonpathogenic p3 peptide, respectively.
Recently, BACE (Beta-site APP Cleaving Enzyme) has been identified as b-secretase. BACE belongs to the family of Aspartyl proteases (Asp) also known as Memapsins. At least four related Asps, located on chromosome IV and X, have been cloned (Asp1, Asp2, Asp3, and Asp4). Human BACE/Asp2/Memapsin2, located on chromosome 11, is a transmembrane protein of 501 aa (signal peptide 1-21 aa, a proprotein domain 22-45 aa, 1 TM domain near the CT, and a short cytoplasmic CT- tail of 24 aa; mature protein 46-460 aa). The lumenal portion of BACE has two active site motifs at 93 aa and 289 aa with signature sequence of aspartic proteases. Rat and mouse BACE (501 aa) are 96% identical with human BACE. BACE expression was most prominent in most areas of the rat brain and pancreas. It has been localized in the compartments of the secretory pathways.
仕様
Size：100ug
Source Antigen：Human
Grade：Highly Purified
Purity：Highly purified
Form：supplied as liquid in PBS, pH 7.4 and 0.1% BSA, 0.02% sodium merthiolate.
