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MilliporeSigma

A1976

Sigma-Aldrich

Anti-Amyloid Peptide β, Cleavage Site 42 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-Aβ 42

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 4 kDa

species reactivity

rat, human, mouse

packaging

antibody small pack of 25 μg

technique(s)

dot blot: 0.05-1 μg/mL
immunoblotting: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: 1:200
radioimmunoassay: 1:200

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

target post-translational modification

proteolytically cleaved (Ala42)

Gene Information

human ... APP(351)
mouse ... App(11820)
rat ... App(54226)

General description

Proteolytic cleavage of the amyloid precursor protein (APP) produces the small fragment amyloid β peptide. Cleavage of APP occurs mostly at residue 40 but to a lesser extent residue 42. Aggregates of amyloid β peptide are found deposited in the brains of Alzheimer′s patients.
Rabbit anti-amyloid peptide β, cleavage site 42 (Aβ42) antibody binds to human, mouse and rat Aβ42.

Immunogen

synthetic peptide of approximately 10 amino acid residues at the C-terminus of Aβ42.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Rabbit anti-Aβ42 is suitable for use in immunoblot, immunohistochemistry, immunoprecipitation, RIA, ELISA and dot blot applications.

Physical form

Solution in phosphate buffer, pH 7.4, containing approximately 25 μg of antibody.

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

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


Certificados de análisis (COA)

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M J Savage et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 18(5), 1743-1752 (1998-03-07)
Fibrillar amyloid deposits are defining pathological lesions in Alzheimer's disease brain and are thought to mediate neuronal death. Amyloid is composed primarily of a 39-42 amino acid protein fragment of the amyloid precursor protein (APP), called amyloid beta-protein (Abeta). Because
Bao-Xi Qu et al.
Vaccine, 28(32), 5280-5287 (2010-06-22)
In an effort to optimize DNA immunization-elicited antibody production responses against A beta 1-42 (A beta 42) as a therapy for Alzheimer's disease (AD), comparisons were made between three distinct plasmid systems using gene gun delivery. Plasmids encoding A beta
Bao-Xi Qu et al.
Journal of the neurological sciences, 260(1-2), 204-213 (2007-06-19)
Abeta42 peptide aggregation and deposition is an important component of the neuropathology of Alzheimer's disease (AD). Gene-gun mediated gene vaccination targeting Abeta42 is a potential method to prevent and treat AD. APPswe/PS1DeltaE9 transgenic (Tg) mice were immunized with an Abeta42
Dietrich E Lorke et al.
BMC neuroscience, 7, 36-36 (2006-04-28)
It has been hypothesized that alterations of the serotonergic system contribute to neuropsychiatric symptoms in Alzheimer disease (AD). Cellular expressions of the two serotonergic receptors 5-HT2A and 5-HT6 have therefore been determined by immunohistochemistry in the prefrontal cortex of patients
Ukjin Kim et al.
Frontiers in pharmacology, 10, 1517-1517 (2020-02-06)
The United States Food and Drug Administration-approved antipsychotic drug, pimozide, has anticancer activities. However, the role of reactive oxygen species (ROS) in its effect on prostate cancer is not well-known. We examined cell proliferation, colony formation, migration, ROS production, and

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