Product Details
| Alternative Name: | β-Secretase 2, β-Site APP-cleaving enzyme 2, Memapsin-1, ASP-1 |
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| Sequence: | aa Ala21-Pro466. |
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| MW: | ~45kDa (calculated); ~48kDa (doublet by SDS-PAGE) |
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| Source: | Produced in insect cells. Recombinant soluble BACE2, cloned from human cDNA, secreted as zymogen from insect cells, purified using a C-terminal His-tag, and cleaved to the mature active form. Produced in a baculovirus expression system. |
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| EC: | 3.4.23.45 |
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| UniProt ID: | Q9Y5Z0 |
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| Formulation: | Liquid. In 50mM TRIS-HCl, pH 7.5, containing 100mM sodium chloride and 20% glycerol. |
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| Purity: | ≥80% (SDS-PAGE) |
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| Purity Detail: | Purified by multi-step chromatography. |
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| Specific Activity: | ≥20 U/µg enzyme. One unit will hydrolyze one pmole Mca-KPLGL-Dpa-AR substrate (Prod. No. BML-P276) (10µM) per minute at 37°C, in 50mM NaOAc, pH 4.5, 1M sodium chloride. |
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| Application Notes: | Useful tool to study enzyme kinetics, cleave target substrates, and screen for BACE2 inhibitors or BACE1 inhibitor selectivity. |
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| Shipping: | Dry Ice |
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| Long Term Storage: | -80°C |
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| Use/Stability: | BACE2 is stable after 5 freeze-thaws at 0.3-0.4 µg/µl; freeze-thaw stability of more dilute preparations has not been tested and could lead to loss of activity. |
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| Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C. |
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| Scientific Background: | BACE2 is an aspartic protease found in both transmembrane and soluble forms. It is related to, and possesses an overlapping substrate profile with, BACE1. It is likely involved in Alzheimer’s disease, and implicated in other neurological, pancreatic, and muscle pathologies. |
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| Regulatory Status: | RUO - Research Use Only |
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SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 1 µg BACE2
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Product Literature References
Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons: M. Pigoni, et al.; Mol. Neurodegener.
11, 67 (2016),
Abstract;
Full Text
The selective BACE1 inhibitor VIa reduces amyloid-β production in cell and mouse models of Alzheimer's disease: X. Cheng, et al.; J. Alzheimers Dis.
37, 823 (2013),
Abstract;
Development of a specific ELISA to measure BACE1 levels in human tissues: A. Gonzales, et al.; J. Neurosci. Methods
202, 70 (2011),
Abstract;
Full Text
General Literature References
BACE1 and BACE2 enzymatic activities in Alzheimer’s disease: R.R. Ahmed, et al.; J. Neurochem.
112, 1045 (2009),
Abstract;
Characterization of a mouse model overexpressing beta-site APP-cleaving enzyme 2 reveals a new role for BACE2: G. Azkona, et al.; Genes Brain Behav.
9, 160 (2009),
Abstract;
BACE2 is stored in secretory granules of mouse and rat pancreatic beta cells: G. Finzi, et al.; Ultrastruct. Pathol.
32, 246 (2008),
Abstract;
Altered beta-secretase enzyme kinetics and levels of both BACE1 and BACE2 in the Alzheimer’s disease brain: J.H. Stockley, et al.; FEBS Lett.
580, 6550 (2006),
Abstract;
BACE1 and BACE2 in pathologic and normal human muscle: G. Vattemi, et al.; Exp. Neurol.
179, 150 (2003),
Abstract;
Specificity of memapsin 1 and its implications on the design of memapsin 2 (beta-secretase) inhibitor selectivity: R.T. Turner 3rd, et al.; Biochemistry
41, 8742 (2002),
Abstract;
Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases: F. Gruninger-Leitch, et al.; J. Biol. Chem.
277, 4687 (2002),
Abstract;
ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site: I. Hussain, et al.; Mol. Cell. Neurosci.
16, 609 (2000),
Abstract;
Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein: X. Lin, et al.; PNAS
97, 1456 (2000),
Abstract;
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