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Key Documents

MABN13

Sigma-Aldrich

Anti-Amyloid β42 Antibody, clone G2-13

clone G2-13, from mouse

Synonyme(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

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About This Item

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

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified antibody

Clone

G2-13, monoclonal

Espèces réactives

human

Réactivité de l'espèce (prédite par homologie)

mouse (based on 100% sequence homology)

Technique(s)

ELISA: suitable
immunohistochemistry: suitable
western blot: suitable

Isotype

IgG1κ

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... APP(351)

Description générale

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. These Amyloid beta antibodies and peptides have been developed as tools for elucidating the biology of AD.

Spécificité

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

Immunogène

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

Application

Anti-Amyloid β42 Antibody, clone G2-13 is an antibody against Amyloid β42 for use in WB, IH, ELISA.
Immunohistochemistry Analysis: 1:300 dilution from a previous lot detected Amyloid β42 in Alzheimerdiseased cerebral cortex and hippocampus tissue.
ELISA: A representative lot of MABN12 antibody was used in a titer ELISA. Specificity of detection for Amyloid beta peptides is displayed below.


ELISA:
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Qualité

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.

Description de la cible

4kDa Calculated

Forme physique

Format: Purified
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 and 1% BSA.

Stockage et stabilité

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

Remarque sur l'analyse

Control
Human Alzheimer diseased brain tissue lysate

Autres remarques

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

Clause de non-responsabilité

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.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Ramune Morkuniene et al.
Journal of neurochemistry, 126(5), 604-615 (2013-06-12)
Beta amyloid (Aβ) oligomers are thought to contribute to the pathogenesis of Alzheimer’s disease. However, clinical trials using Aβ immunization were unsuccessful due to strong brain inflammation, the mechanisms of which are poorly understood. In this study we tested whether

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