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A8978

Sigma-Aldrich

Anti-β-Amyloid (13-28) antibody, Mouse monoclonal

clone BAM90.1, purified from hybridoma cell culture

Synonym(s):

Anti-Aβ

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

BAM90.1, monoclonal

form

buffered aqueous solution

species reactivity

human

packaging

antibody small pack of 25 μL

concentration

~2 mg/mL

technique(s)

enzyme immunoassay: 0.2-0.4 μg/mL using amyloid β-protein
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

Amyloids are insoluble protein aggregates consisting of misfolded proteins and peptides. Amyloid deposition are associated with multiple neurodegenerative disorders.
The β-amyloid precursor protein (APP) is cleaved sequentially by the proteolytic enzymes β-secretase (BACE1) and γ-secretase to produce β-amyloid (Aβ) peptides with the Aβ1-42 and the Aβ1-40 forms being the most prevalent. Secreted Aβ peptides are degraded either via a re-uptake mechanism followed by endosomal degradation, or by an extracellular insulin degrading enzyme. Extracellular accumulation of Aβ leads to the formation of aggregates, fibrils and eventually amyloid deposits called neuritic plaques, which is the hallmark of Alzheimer′s disease (AD).
Monoclonal Anti β-Amyloid [13-28] recognizes the β-Amyloid peptide. The antibody epitope resides within amino acids 20-23.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Mouse Monoclonal Anti-β-Amyloid (13-28) antibody can be used for immunoblotting assays at 1:5,000. The antibody can also be used for IHC, immunoprecipitation,fluorescence infrared spectroscopy and enzyme immunoassays (02-0.4μg/ml).

Physical form

Filtered solution in 0.01 M phosphate buffered saline, pH 7.4.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Amyloid-beta-secondary structure distribution in cerebrospinal fluid and blood measured by an immuno-infrared-sensor: A biomarker candidate for Alzheimer?s disease
Nabers A, et al.
Analytical Chemistry, 88, 2755-2762 (2016)
Julia Stockmann et al.
Alzheimer's research & therapy, 12(1), 169-169 (2020-12-29)
We evaluated Aβ misfolding in combination with Aβ42/40 ratio as a prognostic tool for future clinical progression to mild cognitive impairment (MCI) or dementia due to Alzheimer's disease (AD) in individuals with subjective cognitive decline (SCD). Baseline plasma samples (n = 203)
Andreas Nabers et al.
EMBO molecular medicine, 10(5) (2018-04-08)
Alzheimer's disease (AD) is currently incurable, but there is general agreement that a minimally invasive blood biomarker for screening in preclinical stages would be crucial for future therapy. Diagnostic tools for detection of AD are either invasive like cerebrospinal fluid
Amyloid blood biomarker detects Alzheimer's disease
Nabers A, et al.
EMBO Molecular Medicine, {e8763-{e8763 (2018)
Interactions of pathological hallmark proteins: Tubulin polymerization promoting protein/p25, beta-amyloid and alpha-synuclein
Olah J, et al.
The Journal of Biological Chemistry, jbc-M111 (2011)

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