Alexa Fluor® 594 anti-β-Amyloid, 1-16 Antibody

Pricing & Availability
Clone
6E10 (See other available formats)
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 IgG1
Ave. Rating
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Product Citations
publications
6E10_A594_B-Amyloid_1-16_Antibody_041918
IHC staining of Alexa Fluor® 594 anti-β amyloid, 1-16 antibody (clone 6E10) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using 88% formic acid, the tissue was incubated with 10 µg/ml of the primary antibody overnight at 4°C. The image was captured with a 40X objective. Scale bar: 50 µm
  • 6E10_A594_B-Amyloid_1-16_Antibody_041918
    IHC staining of Alexa Fluor® 594 anti-β amyloid, 1-16 antibody (clone 6E10) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using 88% formic acid, the tissue was incubated with 10 µg/ml of the primary antibody overnight at 4°C. The image was captured with a 40X objective. Scale bar: 50 µm
See Alexa Fluor® 594 spectral data
Cat # Size Price Quantity Avail. Save
803018 25 µg 88€
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803019 100 µg 220€
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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® 594 under optimal conditions. The solution is free of unconjugated Alexa Fluor® 594.
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 residue 1-16 of beta amyloid. The epitope lies within amino acids 3-8 of beta amyloid (EFRHDS).

This antibody clone has been reported for use in immunohistochemistry of free-floating sections2,13.

Application References
  1. Thakker DR, et al. 2009. Proc. Natl. Acad. Sci. USA. 106(11):4501-6. (IHC) PubMed
  2. Oddo S, et al. 2005. Proc. Natl. Acad. Sci. USA. 102(8):3046-51. (IHC-other) PubMed
  3. Herzig M, et al. 2004. Nat. Neuro. 7(9):954-959. (WB) PubMed
  4. Zheng Y, et al. 2012. PLoS One 6:39035. (IHC-F) PubMed
  5. Abramowksi D, et al. J Neurosci. 32:1273. (WB) PubMed
  6. Forny-Germano L, et al. 2014. J. Neurosci. 34:13629. (WB, IHC) PubMed
  7. Gowert NS, et al. 2014. PLoS One 2:e90523. (ICC, EM) PubMed
  8. Sandoval-Hernandez A, et al. 2015. PLoS One. 10: 0145467. (IHC-F)
  9. Kumar R, et al. 2016. Brain. 139:174-92 (WB)
  10. Miyamoto T, et al. 2016. J. Biol. Chem. 291:1719-34. (WB)
  11. Saito S, et al. 2017. Acta Neuropathol. Commun. 5:26-9. (IHC-P) PubMed
  12. Omata Y, et al. 2016. Aging (Albany NY) 8(3):427. (IHC-P) PubMed
  13. Peng W, et al. 2016. Neurobiol. Dis. 93:215. (IHC-other) PubMed
  14. Mandler M, et al. 2015. PLoS One. e0115237. (WB, IHC, ELISA) PubMed
RRID
AB_2734551 (BioLegend Cat. No. 803018)
AB_2734552 (BioLegend Cat. No. 803019)

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 secr
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.
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. 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, 1-16 on UniProt.org

Related FAQs

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Go To Top Version: 2    Revision Date: 05/09/2018

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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