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A1349

Sigma-Aldrich

Monoclonal Anti-β-Amyloid (17-24) antibody produced in mouse

~1 mg/mL, clone 4G8, purified immunoglobulin, buffered aqueous solution

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About This Item

Numero MDL:
Codice UNSPSC:
12352203

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Clone

4G8, monoclonal

Stato

buffered aqueous solution

Reattività contro le specie

human

Concentrazione

~1 mg/mL

tecniche

immunohistochemistry: 1:100-1:1000
immunoprecipitation (IP): 1:10-1:100
indirect ELISA: 1:103-1:105
western blot: 1:100-1:1000

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

Informazioni sul gene

human ... APP(351)

Immunogeno

synthetic peptide corresponding to amino acids 17-24 of the human β amyloid peptide with Glu substituted at position 11, conjugated to KLH.

Stato fisico

Solution in phosphate buffered saline.

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves


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Alina Hategan et al.
Nature structural & molecular biology, 24(4), 379-386 (2017-02-22)
Deposition of amyloid-β plaques is increased in the brains of HIV-infected individuals, and the HIV transactivator of transcription (Tat) protein affects amyloidogenesis through several indirect mechanisms. Here, we investigated direct interactions between Tat and amyloid-β peptide. Our in vitro studies
M Medecigo et al.
Journal of neuroimmunology, 223(1-2), 104-114 (2010-05-11)
Anti-amyloid immunotherapy has been proposed as an appropriate therapeutic approach for Alzheimer's disease (AD). Significant efforts have been made towards the generation and assessment of antibody-based reagents capable of preventing and clearing amyloid aggregates as well as preventing their synaptotoxic
Stefania Zappettini et al.
Frontiers in pharmacology, 3, 146-146 (2012-08-07)
Using both in vitro (hippocampal synaptosomes in superfusion) and in vivo (microdialysis) approaches we investigated whether and to what extent β amyloid peptide 1-40 (Aβ 1-40) interferes with the cholinergic modulation of the release of glycine (GLY) in the rat
Chunyi Jiang et al.
Analytical and bioanalytical chemistry, 396(5), 1745-1754 (2010-02-06)
Aβ(1-42) is the proteolytic cleavage product of cleavage of the amyloid precursor protein by β- and γ-secretases. The aggregation of Aβ(1-42) plays a causative role in the development of Alzheimer's disease. To lock Aβ(1-42) in a homogenous state, we embedded
Jason H Y Yeung et al.
Frontiers in neuroscience, 13, 1427-1427 (2020-02-06)
Alzheimer's disease (AD) is the leading type of dementia worldwide. Despite an increasing burden of disease due to a rapidly aging population, there is still a lack of complete understanding of the precise pathological mechanisms which drive its progression. Glutamate

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