| Product Name | sAPP Beta-w (Highly Sensitive), Human, ELISA Kit |
|---|---|
| Description | Alzheimer's disease (AD) was first reported by A. Alzheimer, a German neuropathologist in 1907 and is considered as a major factor of dementia. It is known that Amyloid b (Ab; which is major constituent of senile plaque) is cleaved from Amyloid Precursor Protein (APP; which exists in three main isoforms, APP695, APP751, and APP770) by b-secretase and subsequent y-secretase (ref. 1). The production of soluble APPb (sAPPb) by b-secretase cleavage corresponds to Ab production accordingly, so it is desired to measure sAPPb in parallel with Ab. In addition, it is reported that APP gene mutation exists in early-onset familial Alzheimer's disease patient. Swedish mutation, one of the APP gene mutations, is a double mutation at positions -1 to -2 from the b-secretase cleavage site (Lys670_Asn and Met671_Leu). And further, it is reported that Swedish mutation elevates Ab40 and Ab42 production (ref. 2), and that the mutation is utilized in establishment of transgenic mice (ref. 3). The measuring sAPPb in Swedish type is useful for research of AD as well as in wild type. On the one hand, it is considered that in the metabolic pathway of APP, APP is first cleaved by a-secretase rather than b-secretase normally to produce soluble APPa (sAPPa) and subsequently P3 is cleaved from the remaining C-terminal fragment by y-secretase. In recent research, there are several attempts to apply the inhibitor of b-secretase and the activation of a-secretase for AD treatment. This kit can measure human soluble sAPPb wild type (sAPPb-w) in samples. This kit is a solid phase sandwich ELISA using 2 kinds of high specific antibodies. Tetra Methyl Benzidine (TMB) is used as a coloring agent (Chromogen). The strength of coloring is proportional to the quantities of Human sAPPb-w. |
| Reactivity | Human |
| Background | Alzheimer's disease (AD) was first reported by A. Alzheimer, a German neuropathologist in 1907 and is considered as a major factor of dementia. It is known that Amyloid b (Ab; which is major constituent of senile plaque) is cleaved from Amyloid Precursor Protein (APP; which exists in three main isoforms, APP695, APP751, and APP770) by b-secretase and subsequent y-secretase (ref. 1). The production of soluble APPb (sAPPb) by b-secretase cleavage corresponds to Ab production accordingly, so it is desired to measure sAPPb in parallel with Ab. In addition, it is reported that APP gene mutation exists in early-onset familial Alzheimer's disease patient. Swedish mutation, one of the APP gene mutations, is a double mutation at positions -1 to -2 from the b-secretase cleavage site (Lys670_Asn and Met671_Leu). And further, it is reported that Swedish mutation elevates Ab40 and Ab42 production (ref. 2), and that the mutation is utilized in establishment of transgenic mice (ref. 3). The measuring sAPPb in Swedish type is useful for research of AD as well as in wild type. On the one hand, it is considered that in the metabolic pathway of APP, APP is first cleaved by a-secretase rather than b-secretase normally to produce soluble APPa (sAPPa) and subsequently P3 is cleaved from the remaining C-terminal fragment by y-secretase. In recent research, there are several attempts to apply the inhibitor of b-secretase and the activation of a-secretase for AD treatment. This kit can measure human soluble sAPPb wild type (sAPPb-w) in samples. |
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