抗Abeta 40抗体 | Anti-Abeta 40 Antibody

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	Western Blot: Abeta 40 Antibody [NB300-225] - Detection of Abeta 40 on 5 ng of peptide per lane using NB300-225. Lane 1: Abeta 40, lane 2: Abeta 42, Lane 3: Abeta 40 and 42 mix.
	Immunocytochemistry/Immunofluorescence: Abeta 40 Antibody [NB300-225] - The Abeta 40 antibody was tested in SH-SY5Y cells at a 1:1000 dilution against Dylight 488 (Green). Alpha tubulin and nuclei were counterstained against Dylight 550 (Red) and DAPI (Blue), respectively.

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Background

Alzheimer's disease (AD) is a devastating neurodegenerative ailment which affects mainly the elderly people and leaves them with progressive intellectual deterioration involving memory, language, judgment, problem solving capability etc. and it is characterized by the accumulation of senile plaques (in brain tissue) composed of amyloid-beta (Abeta) peptides predominantly consisting of 40 (Abeta 40) and 42 (Abeta 42) amino acids which are generated via processing of APP (amyloid precursor protein). APP gets hydrolyzed by beta-secretase to generate a 99-residue membrane-associated C-terminus fragment (APP-C99) which is further cleaved to release a ~4-kDa peptide, Abeta, and AICD (APP intracellular domain) via an unusual form of proteolysis involving gamma-secretase mediated protein cleavage within the transmembrane domain (at residue +40 or +42). On the other hand, alpha-secretase cleaves APP in the middle of the abeta region resulting to the release of a large ectodomain (alpha-APPs), leaveing behind a C-terminus fragment of 83 amino acids (APP-C83) in the membrane which is further cleaved by gamma-secretase to generate p3, an N-terminally truncated form of abeta. The excessive accumulation of abeta peptides in AD is generally due to increased endoproteolytic cleavage of membrane bound APP, over-expression of APP and/or decreased clearance of abeta from the CNS.

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