BACE-2 (Memapsin-1, Beta Secretase-2, ƒÀ-Site Amyloid Precursor Protein-cleaving Enzyme-2) is an aspartic proteinase with a Type-II transmembrane attachment and a cytoplasmic domain. The MEROPS name is Memapsin-2 (Membrane aspartic protease of the pepsin family) The cytoplasmic domain is known to be phosphoregulated, and is involved in the shedding of BACE-2. Different splice variants of BACE-2 exist in humans, the sequences encoding proteins of 518, 468, and 396 amino acids, with predicted masses of 56.2, 50.3, and 43 kDa respectively. Glycosylation and other posttranslational modifications increase their apparent masses on SDS PAGE gels, and BACE-1 is reported as a fuzzy 62-65 kDa band. It is unclear what the relative distribution of the splice variants is, or if the sequences all produce viable proteins. BACE-2 is expressed in the stomach, placenta, pancreas and neuronal tissue, although at lower levels than BACE-1, and is best known for its role in cleaving Amyloid Plaque Protein (APP) at the gƒÀh cleavage site. BACE-2 also cleaves APP at two other sites not cleaved by BACE-1. An aspartic peptidase, BACE-2 uses active sites of DTGS and DGGT, separated by 188 residues in the longest form of BACE-2. The splice variants lead to truncations in the region between the two active sites, relative to the longer form, and the shorter variant lacks a transmembrane domain and has a different carboxyterminus than the other two. The RP3-BACE-2 antibody recognizes the two longest of the splice variants of BACE-2. BACE-2can be found in cell lysates, especially in membrane fractions, and in culture media of cells when the BACE-2 is shed. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species.

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