- Clone
- A18104E (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 nexin-II, peptidase nexin-II, beta-amyloid peptide, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, APP, Amyloid Precursor Protein
- Isotype
- Mouse IgG2b, κ
- Ave. Rating
- Submit a Review
- Product Citations
- publications
![a-A18104E_PURE_BetaAmyloid_Antibody_020723 a-A18104E_PURE_BetaAmyloid_Antibody_020723](https://d1spbj2x7qk4bg.cloudfront.net/Admin/Public/GetImage.ashx?Image=/Files/Images/media_assets/products/product_images/A18104E_PURE_BetaAmyloid_Antibody_020723.png&Width=240&Height=300&altFmImage_path=&Compression=90&Crop=5)
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IHC staining of purified anti-β-amyloid, 17-28 (clone A18104E) on formalin-fixed paraffin-embedded human Alzheimer’s brain tissue. Following antigen retrieval using formic acid, the tissue was incubated with 1.0 µg/mL of the primary antibody overnight at 4°C. Ultra-Streptavidin HRP Kit (Cat. No. 929501) was used for detection followed by hematoxylin counterstaining. The image was captured with a 60X objective. Scale bar: 50 μm -
BSA-conjugated β-amyloid (Aβ) peptides (25 ng total protein) encompassing the C-terminus, middle, and N-terminus regions were resolved by 4-12% Bis-Tris gel electrophoresis, transferred to a PVDF membrane, and probed with 0.5 μg/mL of purified anti-β-Amyloid, 17-28 (clone A18104E) overnight at 4°C. Proteins were visualized by chemiluminescence detection using HRP goat anti-mouse IgG (Cat. No. 405306) at a 1:3000 dilution. Western-Ready™ ECL Substrate Premium Kit (Cat. No. 426319) was used as a detection agent. Lane M: Molecular weight marker
Cat # | Size | Price | Save |
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804601 | 25 µg | ¥31,900 | |
804602 | 100 µg | ¥77,000 |
Alzheimer’s disease is characterized by the accumulation of aggregated amyloid beta (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 DetailsProduct Details
- Verified Reactivity
- Human
- Antibody Type
- Monoclonal
- Host Species
- Mouse
- Immunogen
- Recombinant fragment of human β-Amyloid, 17-28
- Formulation
- Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
- Preparation
- The antibody was purified by affinity chromatography.
- Concentration
- 0.5 mg/mL
- Storage & Handling
- The antibody solution should be stored undiluted between 2°C and 8°C.
- Application
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IHC-P - Quality tested
WB - Verified - Recommended Usage
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Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 1.0 - 10.0 µg/mL is suggested. For western blotting, the suggested use of this reagent is 0.25 - 1.0 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.
- Application Notes
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For use in immunohistochemistry, formic acid antigen retrieval is suggested.
This product is verified in Alzheimer’s disease brain lysate and recombinant human APP751 (Cat. No. 842601) by western blotting. - RRID
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AB_2936738 (BioLegend Cat. No. 804601)
AB_2936738 (BioLegend Cat. No. 804602)
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
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Tissue distribution: Primarily nervous system, but also adipose tissue, intestine, and 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.
- Interaction
- APBA and APBB family
- Biology Area
- Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
- Molecular Family
- APP/β-Amyloid
- Antigen References
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- Kumar A, et al. 2015. Pharmacol Rep. 67:195-203.
- Sadigh-Eteghad S, et al. 2015. Med Princ Pract. 24:1-10.
- Hampel H, et al. 2015. Expert Rev Neruother. 15:83-105.
- Puig KL, et al. 2013. Exp Gerontol. 48:608-11.
- Selkoe DJ, et al. 2016. EMBO Mol Med. 8:595-608.
- Walsh DM, et al. 2007. J Neurochem. 101(5):1172-84.
- Gene ID
- 351 View all products for this Gene ID
- UniProt
- View information about beta-amyloid 17-28 on UniProt.org
Related Pages & Pathways
Pages
Related FAQs
Other Formats
View All β-amyloid 17-28 Reagents Request Custom ConjugationDescription | Clone | Applications |
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Purified anti-β-Amyloid, 17-28 | A18104E | IHC-P,WB |
Compare Data Across All Formats
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.
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Purified anti-β-Amyloid, 17-28
IHC staining of purified anti-β-amyloid, 17-28 (clone A18104... BSA-conjugated β-amyloid (Aβ) peptides (25 ng total protein)...
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