Anti-Amyloid β42 Antibody, clone G2-11

clone G2-11, from mouse

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

Quality Level

biological source



G2-11, monoclonal

species reactivity

human, mouse


ELISA: suitable
immunohistochemistry: suitable
western blot: suitable



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.


This antibody recognizes human Amyloid β42 at the C-terminus.


KLH-conjugated linear peptide corresponding to the C-terminus of Amyloid β42.
Epitope: C-terminus


ELISA: A representative lot of MABN12 antibody was used in a titer ELISA. Specificity of Amyloid beta peptide detection is displayed below.
Research Category
Research Sub Category
Neurodegenerative Diseases
Anti-Amyloid β42 Antibody, clone G2-11 detects level of Amyloid β42 & has been published & validated for use in WB, WB, ELISA, IH.


Evaluated by Western Blot on human Alzheimer diseased brain tissue lysate.

Western Blot Analysis: 1 µg/ml of this antibody detected Amyloid β42 in 10 µg of human Alzheimer diseased brain tissue lysate.

Target description

4 kDa

Physical form

Protein G Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
Format: Purified

Storage and Stability

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

Analysis Note

Human Alzheimer diseased brain tissue lysate

Other Notes

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


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


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Sophia Schedin-Weiss et al.
Alzheimer's research & therapy, 9(1), 57-57 (2017-08-03)
Increased levels of the pathogenic amyloid β-peptide (Aβ), released from its precursor by the transmembrane protease γ-secretase, are found in Alzheimer disease (AD) brains. Interestingly, monoamine oxidase B (MAO-B) activity is also increased in AD brain, but its role in...
Weigang Cui et al.
Molecular medicine reports, 22(2), 739-750 (2020-05-30)
Cognitive impairment and neuro‑inflammatory responses are the distinctive characteristics of Alzheimer's disease (AD). Tormentic acid (TA) is one of the major active components of Potentilla chinensis and has been demonstrated to have anti‑inflammatory properties. However, the potential effects of TA on...
Tina Wahle et al.
Neurochemistry international, 138, 104755-104755 (2020-05-19)
Increasing evidence from toxicological and epidemiological studies indicates that the brain is an important target for ambient (ultrafine) particles. Disturbance of redox-homeostasis and inflammation in the brain are proposed as possible mechanisms that can contribute to neurotoxic and neurodegenerative effects....
Lisa Dolfe et al.
Journal of Alzheimer's disease reports, 2(1), 27-39 (2018-11-28)
Alzheimer's disease (AD) is the most common form of dementia and there is no successful treatment available. Evidence suggests that fibril formation of the amyloid β-peptide (Aβ) is a major underlying cause of AD, and treatment strategies that reduce the...

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