Amyloid Aβ, mouse monoclonal, Cat# MCA-AB9

Amyloid Aβ, mouse monoclonal, Cat# MCA-AB9



Immunohistochemical analysis of paraffin-embedded Alzheimer’s hippocampus using Thioflavin S (left panel) and MCA-AB9 using the HRP-DAB staining technique. Left image shows a section stained with Thioflavin S, a fluorescent reagent which binds to both senile plaques (SP) and neurofibrillary tangles (NFT), the two hallmark lesions of Alzheimer’s disease. Lipofuscin granules (LP) are seen in normal aging brain, but are autofluorescent and so can also be seen in this image. MCA-AB9 show strong staining only of the senile plaques. The right image show MCA-AB9 staining of an adjacent section, showing strong staining of the senile plaques, with more minor staining of blood vessels.

Blot of amyloid beta peptide blotted with MCA-AB9. MCA-AB9 recognizes amyloid β peptide running at 5 kDa and amyloid beta aggregates.

Product name Anti-Amyloid Aβ, A-beta: APP
Description Mouse Monoclonal to Amyloid Aβ, A-beta: APP
Reference Code MCA-AB9
HGNC name APBA2
RRID# AB_2572226
Molecular weight 5 kDa
Immunogen Protein sequence 1-42, epitope is sequence 1-16
Isotype IgG2a
Concentration Antibody is supplied as an aliquot of 1 mg/mL of affinity purified antibody.
Applications Western blot, ICC/IF, IHC
Suggestions for use Western blot: 1:1,000-1:2,000
IF/IHC: 1:1,000.
Storage instructions Shipped on ice. Store at 4°C. For long term storage, leave frozen at -20°C. Avoid freeze / thaw cycles.


Alzheimer’s disease (AD) is a serious and common age related dementia which is characterized by the formation of senile plaques and neurofibrillary tangles. Senile plaques are extracellular accumulations of insoluble proteins found in cortical regions. A major component of senile plaques is β-amyloid, a.k.a. Aβ, a peptide predominantly of 42 or 40 amino acids.

The Aβ peptide is derived from a section of the membrane spanning domain and the immediate extracellular region of a much larger protein called the amyloid precursor protein (APP). This is an abundant protein of poorly understood function.

The Aβ peptides are generated by the activity of proteases called secretases, specifically the β and γ secretases. Certain mutations in the APP gene are associated with familial forms of AD, as are mutations in the genes encoding proteins forming the secretase enzymes, in line with the hypothesis that Aβ accumulation is central to the AD disease process.

Our antibody recognizes amino acids 1-16 of the Aβ peptide and works well on western blots, on formalin fixed sections and as a capture reagent in ELISA. It was originally developed in the Mayo Clinic in Jacksonville in the laboratory of Dr. Todd Golde.


References:

1. Levites, Y., Das, P., Price, R. W., Rochette, M. J., Kostura, L. A., McGowan, E. M., Murphy, M. P., and Golde, T. E. (2006) Anti-Abeta42- and anti-Abeta40-specific mAbs attenuate amyloid deposition in an Alzheimer disease mouse model, The Journal of clinical investigation 116, 193-201.

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