IHC staining of purified anti-β-Amyloid, aggregated antibody (clone A17171C) on formalin-fixed paraffin-embedded normal human (left) and Alzheimer’s disease brain tissue (right). Following antigen retrieval using sodium citrate H.I.E.R, the tissue was incubated with 1 µg/mL of the primary antibody overnight at 4°C. BioLegend’s Ultra Streptavidin (USA) HRP Detection Kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin counterstaining, according to the protocol provided. The images were captured with a 40X objective. Scale bar: 50 µm
IHC staining of purified anti-β-Amyloid, aggregated antibody (clone A17171C) on formalin-fixed paraffin-embedded normal human (left) and Alzheimer’s disease brain tissue (right). Following antigen retrieval using sodium citrate H.I.E.R, the tissue was incubated with 1 µg/mL of the primary antibody overnight at 4°C. BioLegend’s Ultra Streptavidin (USA) HRP Detection Kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin counterstaining, according to the protocol provided. The images were captured with a 40X objective. Scale bar: 50 µm
Western blot of purified anti-β-Amyloid, aggregated antibody (clone A17171C). Lane 1: Molecular weight marker; Lane 2: 20 µg of Tris buffer (pH7.4) extract from Alzheimer’s disease brain; Lane 3: 20 µg of Tris buffer (pH 7.4) extract from normal human brain; Lane 4: 20 µg of Tris/2% SDS buffer extract from Alzheimer’s disease brain; Lane 5: 20 µg of Tris/2% SDS buffer extract from normal human brain. The blot was incubated with 5 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP goat anti-rat IgG antibody (Cat. No. 405405). Enhanced chemiluminescence was used as the detection system.
Western blot of purified anti-β-Amyloid, aggregated antibody (clone A17171C). Lane 1: Molecular weight marker; Lane 2: 2 µg of the human Aβ1-40 peptide; Lane 32 µg of the Aβ1-42 peptide; Lane 4: 25 ng of the recombinant human APP751 protein. The blot was incubated with 2 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP-labeled goat anti-rat IgG (Cat. No. 405405). Enhanced chemiluminescence was used as the detection system.
Alzheimer's disease is characterized by the accumulation of aggregated Aβ peptides in senile plaques and vascular deposits. Aβ peptides are derived from amyloid precursor proteins (APP) through sequential proteolytic cleavage of APP by β-secretases and γ-secretases generating diverse Aβ species. Aβ can aggregate to form soluble oligomeric species and insoluble fibrillar or amorphous assemblies. Some forms of the aggregated peptides are toxic to neurons.
Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 1.0 - 5.0 µg/mL is suggested. For Western blotting, the suggested use of this reagent is 5.0 - 10 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.
Aβ denotes peptides of 36-43 amino acids generated from cleavage of APP by secretases. Aβ has an apparent molecular mass of about 4 kD.
Distribution
Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, and muscle.
Cellular distribution: Cytosol, endosomes, nucleus, plasma membrane, extracellular, and golgi apparatus.
Function
The normal function of Aβ is not well understood. Several potential physiological roles have been proposed, including: activation of kinase enzymes; protection against oxidative stress; regulation of cholesterol transport; transcription factor, and as an anti-microbial agent.
Interaction
Tau, prion, α2-macroglobulin, apoE and apoJ, toll-like receptor 2 (TLR2), TLR4, TLR6, and their co-receptors CD14, CD36, and CD47.
Ligand/Receptor
Receptor for advanced glycation end products (RAGE), low-density lipoprotein receptor-related protein 1 (LRP1), glycoprotein 330 (gp330/megalin), P-glycoprotein.
Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
APP/β-Amyloid
Antigen References
Selkoe DJ. 1994. Annu. Rev. Cell Biol 10:373-403.
O'Brien RJ, Wong PC. 2011. Annu. Rev. Neurosci. 34:185-204.
Chen GF, et al. 2017. Acta. Pharmacol. Sin. 38:1205-1235.
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