IHC staining of Spark YG™ 570 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 5 µg/mL of the primary antibody overnight at 4°C. The slide was mounted with fluoromount G with DAPI. The image was captured with a 40X objective. Scale bar: 50 µm.
IHC staining of Spark YG™ 570 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 5 µg/mL of the primary antibody overnight at 4°C. The slide was mounted with fluoromount G with DAPI. The image was 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.
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 µg/mL is suggested. It is recommended that the reagent be titrated for optimal performance for each application.
* Spark YG™ 570 has a maximum excitation of 555 nm and a maximum emission of 570 nm.
Excitation Laser
Green Laser (532 nm)/Yellow-Green Laser (561 nm)
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-Hernandez 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
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
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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