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Documentos Principais

MABN254

Sigma-Aldrich

Anti-Beta (β)-Amyloid antibody

mouse monoclonal, 6C3

Sinônimo(s):

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

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

Nome do produto

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

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

6C3, monoclonal

reatividade de espécies

human

técnica(s)

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

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... APP(351)

Descrição geral

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.

Especificidade

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

Imunogênio

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

Aplicação

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

Qualidade

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.

Descrição-alvo

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

forma física

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.

Armazenamento e estabilidade

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

Nota de análise

Control
Alzheimer′s diseased human brain tissue.

Outras notas

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Visite a Biblioteca de Documentos

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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