Product 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.
1mg
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): 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
Product Citations: Pontrello CG, et al. 2022. J Alzheimers Dis. 90:1501. PubMed Jury-Garfe N, et al. 2024. Acta Neuropathol. 15:148. PubMed
RRID: AB_2810700 (BioLegend Cat. No. 803023) AB_2810701 (BioLegend Cat. No. 803024)
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: 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
UniProt: View information about beta-Amyloid 1-16 on UniProt.org
Clone: 6E10
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
Q: Do you guarantee that your antibodies are totally pathogen free?
A: 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.
Q: Does BioLegend test each Ultra-LEAF™ antibody by functional assay?
A: 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.
Q: Does BioLegend test each Ultra-LEAF™ antibody for potential pathogens?
A: 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.
Q: Have you tested this Ultra-LEAF™ antibody for in vivo or in vitro applications?
A: 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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Collaboration
Tony Tang
Email: Tony.Tang@iright.com
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