BACE-2 (B-site APP cleaving enzyme 2; also ASP-1 and Memapsin-1) is a 73-75kD member of the peptidase A1 family. It is expressed both inside and outside the CNS and is classified as a Golgi aspartyl protease. Its status as a β-secretase is unclear. If it has physiological activity, it may be associated with glia. Mature BACE-2 is a 456aa type I transmembrane glycoprotein. It contains a 411 aa extracellular domain (aa 63-473) that has two catalytic residues (Asp 93 and Asp 289). Two potential splice forms exist; one shows a deletion of aa's 329-378, while a second shows an 18aa substitution for aa380-518. Over aa63-466, human BACE-2 shares 92% aa sequence identity with mouse BACE-2.
Applications
Suitable for use in ELISA, Western Blot and Immunoprecipitation. Other applications not tested.
Recommended Dilutions
ELISA (Direct): 0.5-1.0ug/ml with the appropriate secondary reagents to detect human and mouse BACE2. The detection limit for BACE-2 is ~0.5ng/well. Western Blot: 0.1-0.2ug/ml with the appropriate secondary reagents to detect human and mouse BACE2. The detection limit for BACE2 is ~5ng/lane and ~25ng/lane under non-reducing and reducing conditions, respectively. Immunoprecipitation: Conditioned media of transfected NS0 cells. Optimal dilutions to be determined by the researcher.
Storage and Stability
Lyophilized and reconstituted products are stable for 12 months after receipt at -20°C. Reconstitute with sterile PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Immunogen
Recombinant protein corresponding to Gly63-Pro466 of human BACE2 derived from NS0 cells.
Form
Supplied as a lyophilized powder from PBS, 5% trehalose. Reconstitute with 500ul sterile PBS.
Purity
Purified by affinity chromatography.
Specificity
Recognizes human BACE2. Species Crossreactivity: mouse. Shows <1% crossreactivity with rhBACE-1, rhCathepsin D, and rhCathepsin E.
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