Western blot of anti-β-amyloid, 1-16 antibody (clone 6E10). Lane 1: Molecular weight marker; Lane 2: 50 ng of the human Aβ1-40 peptide; Lane 3: 50 ng of the Aβ1-42 peptide; Lane 4: 50 ng of the recombinant human APP751 protein; Lane 5: 20 µg of the human brain lysate; Lane 6: 50 ng of the rodent Aβ1-42 peptide. The blot was incubated with 1:10,000 dilution of the primary antibody overnight at 4°C, followed by incubation with the HRP-labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
Western blot of anti-β-amyloid, 1-16 antibody (clone 6E10). Lane 1: Molecular weight marker; Lane 2: 50 ng of the human Aβ1-40 peptide; Lane 3: 50 ng of the Aβ1-42 peptide; Lane 4: 50 ng of the recombinant human APP751 protein; Lane 5: 20 µg of the human brain lysate; Lane 6: 50 ng of the rodent Aβ1-42 peptide. The blot was incubated with 1:10,000 dilution of the primary antibody overnight at 4°C, followed by incubation with the HRP-labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
Direct ELISA of anti-β-amyloid, 1-16 (clone 6E10) antibody binding to the plate-immobilized human Aβ1-40, human Aβ1-42, rodent Aβ1-42 peptides, and recombinant human APP751 protein. ELISA was performed by coating the wells with 100 ng of peptide or recombinant protein. The wells were then incubated with the primary antibody at 37°C for 45 minutes, followed by incubation with HRP labeled goat anti-mouse IgG secondary antibody. TMB (3, 3', 5, 5' tetramethylbenzidine, Cat. No. 421501) was used as the detection system.
IHC staining of anti-β-Amyloid, 1-16 antibody (clone 6E10) on formalin-fixed paraffin-embedded normal human (left panel) and Alzheimer’s disease (right panel)brain tissues. Following antigen retrieval using 70% formic acid for 20 minutes, the tissues were incubated with 1:5,000 dilution of the primary antibody for 1 hour at room temperature. BioLegend’s Ultra-Streptavidin (USA) HRP kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin counterstaining and bluing solution counterstaining, according to the protocol provided. The images were captured with a 40X objective. Scale bar: 50 µm
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.
The concentration is not quantified as this product is sold as undiluted crude mouse ascites fluid. The concentration might vary from lot-to-lot and an estimated concentration would be 1-3 mg/ml.
Storage & Handling
Store at -20°C or below. Upon initial thawing, apportion into working aliquots and store at -20°C or below. Avoid repeated freeze-thaw cycles to prevent denaturing the antibody. Do not store in frost-free freezers.
Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested dilution of this reagent is 1:1,000 to 1:20,000. For Direct ELISA, the suggested dilution of this reagent is 1:10,000 to 1:100,000. For immunohistochemistry on formalin-fixed paraffin-embedded tissue sections, the suggested dilution of this reagent is 1:1,000 to 1:20,000. 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)
Thakker DR, et al. 2009. Proc. Natl. Acad. Sci. USA. 106(11):4501-6. (IHC)PubMed
Oddo S, et al. 2005. Proc. Natl. Acad. Sci. USA. 102(8):3046-51. (IHC-other)PubMed
Herzig M, et al. 2004. Nat. Neuro. 7(9):954-959. (WB)PubMed
Zheng Y, et al. 2012. PLoS One 6:39035. (IHC-F)PubMed
Abramowksi D, et al. J Neurosci. 32:1273. (WB)PubMed
Forny-Germano L, et al. 2014. J. Neurosci. 34:13629. (WB, IHC)PubMed
Gowert NS, et al. 2014. PLoS One 2:e90523. (ICC, EM)PubMed
Sandoval-Hernández A, et al. 2015. PLoS One. 10: 0145467. (IHC-F)
Kumar R, et al. 2016. Brain. 139:174-92 (WB)
Miyamoto T, et al. 2016. J. Biol. Chem. 291:1719-34. (WB)
Saito S, et al. 2017. Acta Neuropathol. Commun. 5:26-9. (IHC-P)PubMed
Omata Y, et al. 2016. Aging (Albany NY) 8(3):427. (IHC-P)PubMed
Peng W, et al. 2016. Neurobiol. Dis. 93:215. (IHC-other)PubMed
Mandler M, et al. 2015. PLoS One. e0115237. (WB, IHC, ELISA)PubMed
Product Citations
Ren X, et al. 2022. J Neuroinflammation. 19:61. PubMed
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
Kumar A, et al. 2015. Pharmacol. Rep. 67(2):195.
Sadigh-Eteghad S, et al. 2015. Med. Princ. Pract. 24(1):1
Hampel H, et al. 2015. Expert Rev. Neurother. 15(1):83.
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