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Purified anti-β-Amyloid, aggregated Antibody

Pricing & Availability
Clone
A18142A (See other available formats)
Regulatory Status
RUO
Other Names
AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, Amyloid beta A4 protein, preA4, protease, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
Isotype
Mouse IgG2b, κ
Ave. Rating
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Product Citations
publications
1_A18142A_PURE_beta-Amyloid_aggregated_Antibody_1_040220_updated.png
Western blot of purified anti-β-Amyloid, aggregated antibody (clone A18142A). Lane 1: Molecular weight marker; Lane 2: 20 µg of Tris buffer (pH7.4) extract from Alzheimer’s disease brain; Lane 3: 20 µg of Tris buffer (pH7.4) extract from normal human brain; Lane 4: 20 µg of Tris/2% SDS buffer extract from Alzheimer’s disease brain; Lane 5: 20 μg of Tris/2% SDS buffer extract from normal human brain; Lane 6: 100 ng APP751 recombinant protein. The blot was incubated with 2 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP goat anti-mouse IgG antibody (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • 1_A18142A_PURE_beta-Amyloid_aggregated_Antibody_1_040220_updated.png
    Western blot of purified anti-β-Amyloid, aggregated antibody (clone A18142A). Lane 1: Molecular weight marker; Lane 2: 20 µg of Tris buffer (pH7.4) extract from Alzheimer’s disease brain; Lane 3: 20 µg of Tris buffer (pH7.4) extract from normal human brain; Lane 4: 20 µg of Tris/2% SDS buffer extract from Alzheimer’s disease brain; Lane 5: 20 μg of Tris/2% SDS buffer extract from normal human brain; Lane 6: 100 ng APP751 recombinant protein. The blot was incubated with 2 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP goat anti-mouse IgG antibody (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • 2_A18142A_PURE_beta-Amyloid_aggregated_Antibody_2_122619.png
    IHC staining of purified anti-β-Amyloid, aggregated antibody (clone A18142A) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using formic acid, the tissue was incubated with 1 µg/mL of the primary antibody overnight at 4°C. BioLegend’s Ultra Streptavidin (USA) HRP Detection Kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin counterstaining, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
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871201 25 µg $129
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871202 100 µg $323
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Description

Alzheimer's disease is characterized by the accumulation of aggregated Aβ peptides in senile plaques and vascular deposits. Aβ peptides are derived from amyloid precursor proteins (APP) through sequential proteolytic cleavage of APP by β-secretases and γ-secretases generating diverse Aβ species. Aβ can aggregate to form soluble oligomeric species and insoluble fibrillar or amorphous assemblies. Some forms of the aggregated peptides are toxic to neurons.

Product Details
Technical data sheet

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Immunogen
Recombinant human amyloid beta (Aβ1-40) protofibrils
Formulation
Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
Preparation
The antibody was purified by affinity chromatography.
Concentration
0.5 mg/mL
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C.
Application

IHC-P - Quality tested
WB - Verified
Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 1 - 10 µg/mL is suggested. For western blotting, the suggested use of this reagent is 2 - 10 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This clone does not cross react with full length APP protein.

RRID
AB_2861107 (BioLegend Cat. No. 871201)
AB_2861107 (BioLegend Cat. No. 871202)

Antigen Details

Structure
Amyloid precursor protein is a 770 amino acid protein with a molecular mass of ~100 kD. According to the UniProtKB database, APP (ID# P05067) has 11 isoforms (34 to ~90 kD) and the 770 form has been designated as the canonical form. Isoform APP695 is the predominant form expressed in neuronal tissue. Isoforms APP751 and APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Aβ denotes peptides of 36-43 amino acids generated from cleavage of APP by secretases. Aβ has an apparent molecular mass of about 4 kD.
Distribution

Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, muscle
Cellular distribution: Cytosol, endosomes, nucleus, plasma membrane, extracellular, and Golgi apparatus

Function
The normal function of Aβ is not well understood. Several potential physiological roles have been proposed, including: activation of kinase enzymes; protection against oxidative stress; regulation of cholesterol transport; transcription factor, and as an anti-microbial agent.
Interaction
Tau, Prion
Cell Type
Neurons
Biology Area
Cell Biology, Neurodegeneration, Neuroinflammation, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
APP/β-Amyloid
Antigen References
  1. Kumar A, et al. 2015. Pharmacol. Rep. 67(2):195.
  2. Sadigh-Eteghad S, et al. 2015. Med. Princ. Pract. 24(1):1.
  3. Hampel H, et al. 2015. Expert Rev. Neurother. 15(1):83.
  4. Puig KL, et al. 2012.  Exp. Gerontol. 48(7): 608.
  5. Selkoe DJ, et al. 2016. EMBO Mol. Med. 8(6):595.
  6. Walsh DM, et al.  2007. J. Neurochem. 101(5):1172.
Gene ID
351 View all products for this Gene ID
UniProt
View information about beta-Amyloid on UniProt.org
Go To Top Version: 1    Revision Date: 12/26/2019

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
If you need assistance with selecting the best format contact our expert technical support team.

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