Alexa Fluor® 647 anti-β-Amyloid, 17-24 Antibody

Pricing & Availability
Clone
4G8 (See other available formats)
Workshop
HCDM listed
Other Names
AAA, ABETA, ABPP, AD1, APPI, CTFgamma, CVAP, PN-II, PN2, Amyloid beta A4 protein, preA4, protease nexin-II, 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
4G8_A647_Beta-Amyloid_Antibody_120717
IHC staining of Alexa Fluor® 647 anti-β-Amyloid, 17-24 antibody (clone 4G8) on formalin-fixed paraffin-embedded normal (A) and Alzheimer’s disease (B) brain tissue. Following antigen retrieval using 88% Formic Acid, the tissues were incubated with 10 µg/ml of the primary antibody overnight at 2-8°C. The tissues were counterstained with DAPI. The images were captured with a 40X objective. Scale bar: 50 µm.
  • 4G8_A647_Beta-Amyloid_Antibody_120717
    IHC staining of Alexa Fluor® 647 anti-β-Amyloid, 17-24 antibody (clone 4G8) on formalin-fixed paraffin-embedded normal (A) and Alzheimer’s disease (B) brain tissue. Following antigen retrieval using 88% Formic Acid, the tissues were incubated with 10 µg/ml of the primary antibody overnight at 2-8°C. The tissues were counterstained with DAPI. The images were captured with a 40X objective. Scale bar: 50 µm.
See Alexa Fluor® 647 spectral data
Cat # Size Price Quantity Avail. Save
800717 25 µg £74
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800718 100 µg £185
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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 (pdf)

Product Details

Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
Preparation
The antibody was purified by affinity chromatography and conjugated with Alexa Fluor® 647 under optimal conditions. The solution is free of unconjugated Alexa Fluor® 647.
Concentration
0.5 mg/ml
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light. Do not freeze.
Application

IHC-P - Quality tested

Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 5.0 - 10.0 µg/ml is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

* Alexa Fluor® 647 has a maximum emission of 668 nm when it is excited at 633 nm / 635 nm.


Alexa Fluor® and Pacific Blue™ are trademarks of Life Technologies Corporation.

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Excitation Laser
Red Laser (633 nm)
Application Notes

This antibody is reactive to amino acid residues 17-24 of β amyloid. The epitope lies within amino acids 18-22 of β amyloid (VFFAE). 4G8 β-amyloid antibody reacts to abnormally processed isoforms, as well as precursor forms.

This antibody clone has been reported for use on IHC of free-floating sections in PBS containing 1% Triton incubated with 0.1 m citrate buffer (4).

Additional reported applications (for the relevant formats) include: immunohistochemical staining on frozen tissue sections (IHC-F) and immunocytochemistry (ICC)

Application References

(PubMed link indicates BioLegend citation)
  1. Poduslo JF, et al. 2004. Biochem. 43:6064. (IHC-F) PubMed
  2. Forny-Germano L, et al. 2014. J Neurosci. 34:13629. (IHC-Other) PubMed
  3. Vallino Costassa E, et al. 2016. J Alzheimers Dis. 51: 875-87. (IHC-P) PubMed
  4. Chen X, et al. 2013. Neurobiol Aging. 34:2370. (ICC) PubMed
  5. Hatami A, et al. 2016. J Alzheimers Dis. 50:517. (IHC-P) PubMed
  6. Kawarabayashi T, et al. 2001. J Neurosci 21:372 (IP)
  7. Fonte V, et al. 2002. PNAS. 110:4853 (IP)
RRID
AB_2721295 (BioLegend Cat. No. 800717)
AB_2721296 (BioLegend Cat. No. 800718)

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, and 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.
Biology Area
Cell Biology, Neurodegeneration, 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 Neruother. 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, 17-24 on UniProt.org

Related FAQs

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Go To Top Version: 1    Revision Date: 12/11/2017

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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