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Key Documents

MABN254

Sigma-Aldrich

Anti-amyloid beta peptide (MOAB-2), pan Antibody, clone 6C3

clone 6C3, from mouse

Sinónimos:

Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer′s disease amyloid protein, cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

6C3, monoclonal

species reactivity

human

technique(s)

dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

Pan-amyloid-beta (1-40) is one of several functional peptides (39 to 43 amino acids in length) formed from proteolytic cleavage of the amyloid-beta precursor protein (APP) by the family of secretase enzymes. Although the APP protein is required for a number of biological functions, including axonal transport, cell adhesion, and transcription, the Ab 1-40 peptide has been studied mostly for its potential to aggregate and form neurite plaques, which may contribute to neurotoxicity, particularly in the context of neurodegenerative disease such as Alzheimer’s. Previous studies have demonstrated that Anti-pan amyloid beta peptide (MOAB2), clone 6C3 detects specifically amyloid-beta, but not APP. Furthermore MOAB2 detects multiple amyloid-beta 40 and amyloid-beta 42 conformations including unaggregated, oligomeric and fibrillar. In a number of immunohistochemical and biochemical analyses, MOAB2 consistently detected intraneuronal amyloid-beta, but not APP, and showed greater specificity to amyloid-beta than 6E10. MOAB2 is therefore suitable for sensitive and specific detection of accumulating amyloid-beta peptides in Alzheimer’s disease models.

Specificity

This antibody recognizes amyloid-ß and not APP (amyloid precursor protein). Specifically, clone 6C3 recognizes unaggregated, oligomeric, and fibrillar forms of Aß42 and Aß40.

Immunogen

Linear peptide corresponding to human pan amyloid beta peptide (MOAB-2).

Application

Anti-amyloid beta peptide (MOAB-2), pan Antibody, clone 6C3 is an antibody against amyloid beta peptide (MOAB-2), pan, clone 6C3 for use in western blotting, IHC (Paraffin), Immunofluorescence, IP, Dot Blot.
Immunofluorescence Analysis: A 1:1,000 dilution from a representative lot detected Amyloid Beta Peptide in human Alzeimer′s diseased brain (see website for images).

Western Blot Analysis: A representative lot was used by an independent laboratory in unaggregated forms of Aß42 and Aß40. (Youmans, K.L., et al. (2012). Mol Neurodegener. 7;8.)

Dot Blot Analysis: Serial Aβ40 and Aβ42 dilutions were probed with MOAB-2 or 6E10 by an independent laboratory. (Youmans, K.L., et al. (2012). Mol Neurodegener. 7;8.)

Immunoprecipitationt Analysis: A representative lot was used by an independent laboratory in unaggregated and fibrillar forms of Aß42 and Aß40. (Youmans, K.L., et al. (2012). Mol Neurodegener. 7;8.)
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Quality

Evaluated by Immunohistochemistry in Alzheimer′s diseased human brain tissue.

Immunohistochemistry Analysis: A 1:1,000 dilution of this antibody detected Amyloid Beta Peptide in human Alzheimer′s diseased brain tissue.

Target description

4 kDa calculated but could be larger since clone 6C3 recognizes unaggregated, oligomeric, and fibrillar forms of Aß42 and Aß40.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aλ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

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

Analysis Note

Control
Alzheimer′s diseased human brain tissue.

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Katherine L Youmans et al.
Molecular neurodegeneration, 7, 8-8 (2012-03-20)
The form(s) of amyloid-β peptide (Aβ) associated with the pathology characteristic of Alzheimer's disease (AD) remains unclear. In particular, the neurotoxicity of intraneuronal Aβ accumulation is an issue of considerable controversy; even the existence of Aβ deposits within neurons has
Natalia A Muraleva et al.
Antioxidants (Basel, Switzerland), 9(8) (2020-08-01)
Alzheimer's disease (AD) is the most common type of dementia and is currently incurable, and mitogen-activated protein kinase (MAPK) p38 is implicated in the pathogenesis of AD. p38 MAPK inhibition is considered a promising strategy against AD, but there are
Xu Hou et al.
Frontiers in aging neuroscience, 7, 207-207 (2015-11-20)
Alzheimer's disease (AD), the most common form of dementia, disproportionately affects women in both prevalence and severity. This increased vulnerability to AD in women is strongly associated with age-related ovarian hormone loss and apolipoprotein E 4 allele (ApoE4), the most
Cinzia Rinaldo et al.
Cancer research, 69(15), 6241-6248 (2009-07-30)
In the past few years, much effort has been devoted to show the single-target specificity of nongenotoxic, p53 reactivating compounds. However, the divergent biological responses induced by the different compounds, even in the same tumor cells, demand additional mechanistic insights
Natalia A Stefanova et al.
Aging, 8(11), 2713-2733 (2016-10-18)
Mitochondrial aberrations are observed in human Alzheimer's disease (AD) and in medical conditions that increase the risk of this disorder, suggesting that mitochondrial dysfunction may contribute to pathophysiology of AD. Here, using OXYS rats that simulate key characteristics of sporadic

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