Biotin anti-β-Amyloid, 1-16 Antibody (Previously Covance catalog# SIG-39340)

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
Previously
Signet Catalog# 9340-02
Signet Catalog# 9340-05
Signet Catalog# 9340-10
Covance Catalog# SIG-39340
Isotype
Mouse IgG1, κ
6E10_Biotin_beta-Amyloid_Antibody_012319_updated.png
IHC staining of biotin 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 10 µg/ml of the primary antibody for 60 minutes at room temperature. For detection, the HRP labeling reagent and DAB from BioLegend's Ultra Streptavidin (USA) HRP Detection Kit were used (Ultra Streptavidin (USA) HRP Detection Kit (Multi-Species, DAB); Cat. No. 929901). Slides were counterstained with hematoxylin, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
  • 6E10_Biotin_beta-Amyloid_Antibody_012319_updated.png
    IHC staining of biotin 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 10 µg/ml of the primary antibody for 60 minutes at room temperature. For detection, the HRP labeling reagent and DAB from BioLegend's Ultra Streptavidin (USA) HRP Detection Kit were used (Ultra Streptavidin (USA) HRP Detection Kit (Multi-Species, DAB); Cat. No. 929901). Slides were counterstained with hematoxylin, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
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803007 200 µL $654.00
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803008 500 µL $1292.00
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803009 1 mL $2284.00
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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.

Technical data sheet

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution; no preservatives or carrier proteins.
Preparation
The antibody was purified by affinity chromatography.
Concentration
1 mg/mL
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C. Please note the storage condition for this antibody has been changed from -20°C to between 2°C and 8°C. You can also check your vial or your CoA to find the most accurate storage condition for this antibody.
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 1.0 - 10 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-Hernández 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. Alfonso S, et al. 2016. Sci Signal. 9: ra47. PubMed
  2. Sompol P, et al. 2021. Aging Cell. :e13416. PubMed
  3. Braun DJ, et al. 2023. PLoS One. 18:e0286495. PubMed
  4. Jiang Z, et al. 2022. Anesth Analg. 641:135. PubMed
  5. Karaahmet B, et al. 2023. Pharmaceutics. :15. PubMed
  6. Mateus A, et al. 2017. Proc Natl Acad Sci U S A. 114:E6231. PubMed
  7. Chen JF, et al. 2021. Neuron. . PubMed
  8. Larson M, et al. 2012. J Neurosci. 32:10253-10266. PubMed
  9. Chiang ACA, et al. 2018. Am J Pathol. 188:739. PubMed
  10. Sompol P et al. 2017. The Journal of Neuroscience. 37(25):6132-6148 . PubMed
  11. Osborne C, et al. 2018. J Cell Sci. 131:. PubMed
  12. Zhou Z, et al. 2017. J Neuroinflammation. 14:75. PubMed
  13. Sherman M, et al. 2016. J Neurosci. 36: 9647 - 9658. PubMed
  14. Grant MKO, et al. 2019. PLoS One. 14:e0212815. PubMed
  15. Fitz NF, et al. 2020. Mol Neurodegener. 15:41. PubMed
  16. Chernick D, et al. 2018. J Neurochem. 147:647. PubMed
  17. Duncan MJ, et al. 2019. Alzheimers Dement (N Y). 5:70. PubMed
  18. Carter A, et al. 2017. PLoS One. 12(2):e0172161. PubMed
  19. Lathuilière A, et al. 2016. Brain. 10.1093/brain/aww036. PubMed
  20. Thygesen C, et al. 2018. Front Cell Neurosci. 12:397. PubMed
  21. West E, et al. 2017. J Cell Sci. 130:3050. PubMed
  22. Metaxas A, et al. 2019. Front Cell Neurosci. 0.915277778. PubMed
RRID
AB_2564656 (BioLegend Cat. No. 803007)
AB_2564656 (BioLegend Cat. No. 803008)
AB_2564656 (BioLegend Cat. No. 803009)

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.
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
Go To Top Version: 6    Revision Date: 03/12/2021

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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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