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Alexa Fluor® 594 anti-β-Amyloid, 17-24 Antibody

Pricing & Availability
Clone
4G8 (See other available formats)
Regulatory Status
RUO
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_A594_Beta-Amyloid_Ascites_Antibody_120717
IHC staining of Alexa Fluor® 594 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 tissue was incubated with 5 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_A594_Beta-Amyloid_Ascites_Antibody_120717
    IHC staining of Alexa Fluor® 594 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 tissue was incubated with 5 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.
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800715 25 µg 104€
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800716 100 µg 259€
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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

Verified Reactivity
Human, Mouse
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® 594 under optimal conditions.
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® 594 has an excitation maximum of 590 nm, and a maximum emission of 617 nm.


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

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Application Notes

This antibody is reactive to amino acid residues 17-24 of ß amyloid. The epitope lies within amino acids 18-22 of ß amyloid (VFFAE). 4G8 ß-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)
Product Citations
  1. Gopalakrishna R, et al. 2022. FEBS Lett. 596:2914. PubMed
RRID
AB_2721292 (BioLegend Cat. No. 800715)
AB_2721292 (BioLegend Cat. No. 800716)

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
Go To Top Version: 2    Revision Date: 12/16/2021

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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