- 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
- Mouse IgG1
- Ave. Rating
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- Product Citations
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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
- Antibody Type
- Host Species
- 0.2 µm filtered in phosphate-buffered solution, pH 7.2, containing no preservative. Endotoxin level is <0.01 EU/µg of the protein (<0.001 ng/µg of the protein) as determined by the LAL test.
- The Ultra-LEAF™ (Low Endotoxin, Azide-Free) antibody was purified by affinity chromatography.
- 1.0 mg/ml
- 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.
WB - Quality tested
IHC-P - Validated
ICC, IHC-F, EM - Reported in literature
- 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.
(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 secretases. Aβ has an apparent molecular mass of about 4 kD.
Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, and muscle.
Cellular distribution: Cytosol, endosomes, nucleus, plasma membrane, extracellular, and golgi apparatus.
- 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
- 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.
- Puig KL, et al. 2012. Exp. Gerontol. 48(7): 608.
- Selkoe DJ, et al. 2016. EMBO Mol. Med. 8(6):595.
- Walsh DM, et al. 2007. J. Neurochem. 101(5):1172.
- Gene ID
- 351 View all products for this Gene ID
- View information about beta-Amyloid, 1-16 on UniProt.org
- Does BioLegend test each LEAF™ antibody by functional assay?
No, BioLegend does not test 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.
- 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 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 LEAF™/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.
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