MABN11

Sigma-Aldrich

Anti-Amyloid β40 Antibody, clone G2-10

clone G2-10, from mouse

Synonym(s):
Alzheimer disease, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, Protease nexin-II, amyloid beta (A4) precursor protein, amyloid beta A4 protein, amyloid beta precursor protein, beta-amyloid peptide, human mRNA for amyloid A4 prec
eCl@ss:
32160702
NACRES:
NA.41
Pricing and availability is not currently available.

Quality Level

biological source

mouse

clone

G2-10, monoclonal

species reactivity

human, mouse

application(s)

ELISA: suitable
immunohistochemistry: suitable
western blot: suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

Gene Information

human ... APP(351)

General description

The cerebral and vascular plaques associated with Alzheimer′s disease (AD) are mainly composed of amyloid beta peptides (Aβ). Aβ is derived from cleavage of the amyloid precursor protein (APP) and varies in length from 39 to 43 amino acids. Aβ [1-40], Aβ [1-42], and Aβ [1-43] peptides result from cleavage of APP after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last APP processing step. Aβ [1-40], [1-42] and [1-43] peptides are major constituents of the plaques and tangles that occur in AD. Aβ antibodies and peptides have been developed as tools for elucidating the biology of AD.

Specificity

This antibody recognizes Amyloid β40 at the C-terminus.

Immunogen

Linear peptide of human Amyloid β40 at the C terminus.
Epitope: C-terminus

Application

Immunohistochemistry Analysis: 1:300 dilution from a previous lot detected Amyloid β40 in Alzheimer’s diseased hippocampus tissue.
Detect Amyloid β40 using this Anti-Amyloid β40 Antibody, clone G2-10 validated for use in WB, IH, ELISA.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Quality

Evaluated by Western Blot in APP transgenic CRND8 mouse brain lysate.

Western Blot Analysis: 1 µg/ml of this antibody detected Amyloid β40 on 10 µg of APP transgenic CRND8 mouse brain lysate.

Target description

~ 4 kDa

Physical form

Protein G Purified
Purified mouse monoclonal IgG2bκ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide and 1% BSA.
Format: Purified

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
APP transgenic CRND8 mouse brain lysate

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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.

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Ditte Z Christensen et al.
Frontiers in aging neuroscience, 6, 139-139 (2014-07-16)
Abnormalities and impairments in axonal transport are suggested to strongly contribute to the pathological alterations underlying AD. The exact mechanisms leading to axonopathy are currently unclear, but it was recently suggested that APP expression itself triggers axonal degeneration. We used...
Ge Li et al.
International journal of molecular medicine, 42(4), 1935-1944 (2018-08-08)
Aging is associated with impairment of the paravascular pathway caused by the activation of astrocytes and depolarization of protein aquaporin‑4 (AQP4) water channels, resulting in the accumulation of protein waste, including amyloid β (Aβ), in the brain parenchyma. The secreted...
Jin Cui et al.
Cell discovery, 1, 15021-15021 (2015-01-01)
Despite decades of intense global effort, no disease-modifying drugs for Alzheimer's disease have emerged. Molecules targeting catalytic activities of γ-secretase or β-site APP-cleaving enzyme 1 (BACE1) have been beset by undesired side effects. We hypothesized that blocking the interaction between...

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