Skip to Content
Merck
All Photos(1)

Key Documents

MABN639

Sigma-Aldrich

Anti-Amyloid βA4, clone 1E8 (Amino Terminus) Antibody

clone 1E8, 1 mg/mL, from mouse

Synonym(s):

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

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

mouse

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

1E8, monoclonal

purified by

affinity chromatography

species reactivity

human

concentration

1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1κ

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... APP(351)

General description

Amyloid beta A4 protein, also known as ABPP or APPI (APP) or Alzheimer disease amyloid protein or Cerebral vascular amyloid peptide (CVAP) or PreA4 or Protease nexin-II (PN-II), and encoded by the gene name APP or A4 or AD1, belongs to the APP family. The beta-amyloid peptide (beta A4), proteolytically released from the amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer′s disease. Cleavage of APP by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Mab βA4N-1E8 recognizes the free N-terminus of the bA4 polypeptide with high preference and crossreacts with sAPPα.

Specificity

This antibody is specific for the first 2 amino acids of the Amyloid beta peptide amino terminus.

Immunogen

Epitope: N-terminus
KLH-conjugated peptide corresponding to the N-terminus of human Amyloid βA4.

Application

Immunohistochemistry Analysis: A 1:500-2,000 dilution from a representative lot was used to detect Amyloid βA4 in human Alzheimer′s brain and thalamus tissues.

Western Blotting Analysis: A representative lot was used to detect Amyloid βA4 in Western Blotting. (Wiltfang, et al. 2001; Serneels, et al. 2009; Maler, et al. 2007).

Immunoprecipitation Analysis: A representative lot was used to detect Amyloid βA4 in Immunoprecipitation. (Wiltfang, et al. 2001; Maler, et al. 2007).
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
This Anti-Amyloid βA4, clone 1E8 (Amino Terminus) Antibody is validated for use in western blotting, IHC & IP for the detection of Amyloid βA4.

Quality

Evaluated by Western Blotting in human Alzheimer′s brain tissue lysate.

Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Amyloid βA4 in human Alzheimer′s brain tissue lysate.

Target description

~4 kDa observed. Uncharacterized bands may be observed in some lysate(s).

Physical form

Affinity
Purified mouse monoclonal IgG1κ in buffer containing PBS, PEG, Sucrose, and up to 0.1% sodium azide.

Storage and Stability

For long-term storage, freeze lyophilizate upon arrival (2-8°C). Upon reconstitution, aliquote and freeze in liquid nitrogen; reconstituted antibody can be stored frozen at -80°C up to 1 year. Thaw aliquots at 37°C. Thawed aliquots may be stored at 4°C up to 3 months.

Avoid repeated freeze / thaw cycles.

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.

Not finding the right product?  

Try our Product Selector Tool.

Pictograms

Skull and crossbones

Signal Word

Danger

Hazard Statements

Hazard Classifications

Acute Tox. 3 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 1


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Lauren H Fairley et al.
Proceedings of the National Academy of Sciences of the United States of America, 120(8), e2209177120-e2209177120 (2023-02-15)
Microglial phagocytosis is an energetically demanding process that plays a critical role in the removal of toxic protein aggregates in Alzheimer's disease (AD). Recent evidence indicates that a switch in energy production from mitochondrial respiration to glycolysis disrupts this important
Daniela Giraldo-Berrio et al.
Neurotoxicity research, 42(3), 28-28 (2024-06-06)
Parkinson's disease with dementia (PDD) is a neurological disorder that clinically and neuropathologically overlaps with Parkinson's disease (PD) and Alzheimer's disease (AD). Although it is assumed that alpha-synuclein ( α -Syn), amyloid beta (A β ), and the protein Tau
Nicolas Gomez-Sequeda et al.
International journal of molecular sciences, 25(9) (2024-05-11)
Familial Alzheimer's disease (FAD) is a complex and multifactorial neurodegenerative disorder for which no curative therapies are yet available. Indeed, no single medication or intervention has proven fully effective thus far. Therefore, the combination of multitarget agents has been appealing

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service