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Ultra-LEAF™ Purified anti-β-Amyloid, 1-16 Antibody

Pricing & Availability
Clone
6E10 (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 IgG1, κ
Ave. Rating
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Product Citations
publications
6E10_LEAF_B-Amyloid1-16_Antibody_1_102218
Western blot of Ultra-LEAF™ Purified anti-β-Amyloid, 1-16 antibody (clone 6E10). Lane 1: Molecular weight marker; Lane 2: 10 ng of the recombinant human APP770 protein; Lane 3: 50 ng of the human Aβ1-40 peptide; Lane 4: 50 ng of the human Aβ1-42 peptide; Lane 5: 50 µg of normal human brain lysate; Land 6: 50 µg of Alzheimer's disease human brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • 6E10_LEAF_B-Amyloid1-16_Antibody_1_102218
    Western blot of Ultra-LEAF™ Purified anti-β-Amyloid, 1-16 antibody (clone 6E10). Lane 1: Molecular weight marker; Lane 2: 10 ng of the recombinant human APP770 protein; Lane 3: 50 ng of the human Aβ1-40 peptide; Lane 4: 50 ng of the human Aβ1-42 peptide; Lane 5: 50 µg of normal human brain lysate; Land 6: 50 µg of Alzheimer's disease human brain lysate. The blot was incubated with 1 µg/mL of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • 6E10_LEAF_B-Amyloid1-16_Antibody_2_102218
    IHC staining of Ultra-LEAF™ Purified anti-β-Amyloid, 1-16 antibody (clone 6E10) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using 88% formic acid for 20 minutes at room temperature, the tissue was incubated with 1 µg/ml of the primary antibody for 60 minutes at room temperature. BioLegend´s Ultra-Streptavidin (USA) HRP 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
  • 6E10_LEAF_B-Amyloid1-16_Antibody_3_102218
    IHC staining of Ultra-LEAF™ Purified anti-β-Amyloid, 1-16 antibody (clone 6E10) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using 88% formic acid for 20 minutes at room temperature, the tissue was incubated with 1 µg/ml of the primary antibody for 60 minutes at room temperature. BioLegend´s Ultra-Streptavidin (USA) HRP 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 10X objective. Scale bar: 50 µm
Compare all formats
Cat # Size Price Save
803023 100 µg ¥55,780
803024 1 mg ¥333,000

Select size of product is eligible for a 40% discount! Promotion valid until December 31, 2024. Exclusions apply. To view full promotion terms and conditions or to contact your local BioLegend representative to receive a quote, visit our webpage.

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
Formulation
0.2 µm filtered in phosphate-buffered solution, pH 7.2, containing no preservative.
Endotoxin Level
Less than 0.01 EU/µg of the protein (< 0.001 ng/µg of the protein) as determined by the LAL test.
Preparation
The Ultra-LEAF™ (Low Endotoxin, Azide-Free) antibody was purified by affinity chromatography.
Concentration
The antibody is bottled at the concentration indicated on the vial, typically between 2 mg/mL and 3 mg/mL. Older lots may have also been bottled at 1 mg/mL. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C. This Ultra-LEAF™ solution contains no preservative; handle under aseptic conditions.
Application

WB - Quality tested
IHC-P - Verified
ICC, IHC-F, EM - Reported in the literature, not verified in house
Recommended Usage

Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested use of this reagent is 0.2 - 1.0 µg per mL. For immunohistochemistry on formalin-fixed paraffin-embedded tissue, a concentration range of 0.2 - 5.0 µg/mL is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

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

(PubMed link indicates BioLegend citation)
  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
Product Citations
  1. Pontrello CG, et al. 2022. J Alzheimers Dis. 90:1501. PubMed
RRID
AB_2810701 (BioLegend Cat. No. 803023)
AB_2810701 (BioLegend Cat. No. 803024)

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

Do you guarantee that your antibodies are totally pathogen free?

BioLegend does not test for pathogens in-house aside from the GoInVivo™ product line. However, upon request, this can be tested on a custom basis with an outside, independent laboratory.

Does BioLegend test each Ultra-LEAF™ antibody by functional assay?

No, BioLegend does not test Ultra-LEAF™ antibodies by functional assays unless otherwise indicated. Due to the possible complexities and variations of uses of biofunctional antibodies in different assays and because of the large product portfolio, BioLegend does not currently perform functional assays as a routine QC for the antibodies. However, we do provide references in which the antibodies were used for functional assays and we do perform QC to verify the specificity and quality of the antibody based on our strict specification criteria.

Does BioLegend test each Ultra-LEAF™ antibody for potential pathogens?

No, BioLegend does not test for pathogens in-house unless otherwise indicated.  However, we can recommend an outside vendor to perform this testing as needed.

Have you tested this Ultra-LEAF™ antibody for in vivo or in vitro applications?

We don't test our antibodies for in vivo or in vitro applications unless otherwise indicated. Depending on the product, the TDS may describe literature supporting usage of a particular product for bioassay. It may be best to further consult the literature to find clone specific information.

Go To Top Version: 2    Revision Date: 03/12/2021

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.

 

BioLegend, the BioLegend logo, and all other trademarks are property of BioLegend, Inc. or their respective owners, and all rights are reserved.

 

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Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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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