- Clone
- A18114B (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, 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
Cat # | Size | Price | Quantity Check Availability | Save | ||
---|---|---|---|---|---|---|
871301 | 25 µg | $129 | ||||
871302 | 100 µg | $323 |
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 DetailsProduct Details
- Verified Reactivity
- Human
- Antibody Type
- Monoclonal
- Host Species
- Mouse
- Immunogen
- Human amyloid beta fibrils
- 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
-
IHC-P - Quality tested
WB - Verified - Recommended Usage
-
Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 0.5 - 10 µg/mL is suggested. For western blotting, the suggested use of this reagent is 2.0 - 10 µg/mL. It is recommended that the reagent be titrated for optimal performance for each application.
- Application Notes
-
This clone detects full length APP.
- RRID
-
AB_2832880 (BioLegend Cat. No. 871301)
AB_2832880 (BioLegend Cat. No. 871302)
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
-
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.
- Interaction
- Tau, Prion
- Cell Type
- Neurons
- Biology Area
- Cell Biology, Neurodegeneration, Neuroinflammation, 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 & Combs CK. 2012. Exp Gerontol. 48(7): 608.
- Selkoe DJ & Hardy J. 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
- UniProt
- View information about beta-Amyloid on UniProt.org
Other Formats
View All β-Amyloid Reagents Request Custom ConjugationDescription | Clone | Applications |
---|---|---|
Purified anti-β-Amyloid, aggregated | A18114B | IHC-P,WB |
Compare Data Across All Formats
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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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