ABN454-I
Anti-Tau (T22) Antibody, oligomeric
from rabbit, purified by affinity chromatography
Sign Into View Organizational & Contract Pricing
All Photos(4)
Microtubule-associated protein tau oligomer, Tau oligomer, PHF-tau oligomer, Paired helical filament-tau oligomer, Neurofibrillary tangle protein oligomer
Recommended Products
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human
technique(s)
dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
ambient
target post-translational modification
unmodified
Gene Information
human ... MAPT(4137)
General description
Microtubule-associated protein tau (UniProt P10636; also known as Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau) is encoded by the MAPT (also known as TAU, MAPT1, MTBTL) gene (Gene ID 4137) in human. In Alzheimer′s disease (AD) pathology, accumulation of the microtubule-associated protein tau takes place primarily in the neurons. Tau accumulates in both the somatodendritic and axonal domains of neurons. Tau also accumulates in the soma as neurofibrillary tangles (NFTs). Cell death and synaptic lesions occur independently of NFT formation, and research indicates that NFT formation alone is insufficient for neurodegeneration, suggesting that soluble tau aggregates may be the more toxic and pathologically significant tau species. Tau oligomers are neurotoxic when applied extracellularly to cultured neuronal cells, and tau oligomers (but not fibrils) induce neurodegeneration and synaptic and mitochondrial dysfunction in vivo. Moreove, researchers are able to use tau oligomers as a reliable biomarker to differentiate AD brains from age-matched non-AD brains.
Specificity
T22 specifically recognizes and neutralizes oligomeric tau, T22 does not show any significant reactivity toward monomeric tau, tau fibrils, Aβ oligomers, Aβ fibrils, α-synuclein oligomers, or α-synuclein fibrils (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunogen
Recombinant human Tau-441 (Tau-F, Tau-4, 2N4R isoform) oligomers (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Application
Research Category
Neuroscience
Neuroscience
This rabbit polyclonal Anti-Tau (T22), oligomeric, Cat. No. ABN454-I detects levels of Tau oligomers, and has been published and validated for use in Dot Blot, Immunofluorescence, Immunohistochemistry and Western Blotting.
Western Blotting Analysis: 4-6.67 µg/mL from a representative lot detected tau oligomers in frontal cortex tissue lysates from Alzheimer′s diseased (AD), but not from age-matched non-AD, human brains (Courtesy of Prof. Rakez Kayed, University of Texas, Galveston).
Dot Blot Analysis: A representative lot detected human P301S tau oligomers in hippocampal dentate gyrus (DG) and medial entorhinal cortex (MEC) tissue lysates from PS19 transgenic mice. Daily N-SMase Inhibitor GW4869 i.p. injection reduced tau oligomer accumulation in DG, but not MEC (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
Dot Blot Analysis: A representative lot detected increased tau oligomers formation in Alzheimer′s diseased (AD) as well as in aged non-AD human medial temporal gyrus tissue lysates (Blair, L.J., et al. (2013). J. Clin. Invest. 123(10):4158-4169).
Immunohistochemistry Analysis: A representative lot detected human tau oligomers formation in paraffin-embedded striatal sections of Huntington s diseased brains (Vuono, R., et al. (2015). Brain. 138(Pt 7):1907-1918).
Immunohistochemistry Analysis: A representative lot detected increased human tau P301L mutant oligomers formation in CA3 region of Tg4510 mice following FKBP51-expressing AAV viarl particles injection using 4% paraformaldehyde-fixed free-floating brain sections (Blair, L.J., et al. (2013). J. Clin. Invest. 123(10):4158-4169).
Immunofluorescence Analysis: A representative lot detected granule cell layer (GCL) neurons containing oligomers of virally expressed human P301L mutant tau 1 441 by fluorescent immunohistochemistry staining of brain sections from mice received recombinant viral injection to the medial entorhinal cortex (MEC) (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
Immunofluorescence Analysis: A representative lot detected greatly enhanced tau oligomers co-localized with that of oxidative nucleic acid damage marker 8-OH(d)G in human AD brain, as well as heat stress- (HS-) induced Tau oligomers formation in the brain CA1 region of THY-Tau22 transgenic mice expressing human tau with G272V and P301S mutation by fluorescent immunohistochemistry staining of paraffin-embedded brain tissue sections (Violet, M., et al. (2015). Neurobiol. Dis. 82:540-551).
Western Blotting Analysis: A representative lot detected human P301S tau oligomers-containing exosomal fractions from PS19 transgenic mice. Dietary supplementation with CSF-1R Inhibitor PLX3397 reduced exosomal tau oligomer accumulation (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
The unpurified antiserum (Cat. No. ABN454) is also available for dot blot, ELISA, immunofluorescence, immunohistochemistry, immunoprecipitation, neutralization, and Western blotting applications.
Dot Blot Analysis: A representative lot detected human P301S tau oligomers in hippocampal dentate gyrus (DG) and medial entorhinal cortex (MEC) tissue lysates from PS19 transgenic mice. Daily N-SMase Inhibitor GW4869 i.p. injection reduced tau oligomer accumulation in DG, but not MEC (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
Dot Blot Analysis: A representative lot detected increased tau oligomers formation in Alzheimer′s diseased (AD) as well as in aged non-AD human medial temporal gyrus tissue lysates (Blair, L.J., et al. (2013). J. Clin. Invest. 123(10):4158-4169).
Immunohistochemistry Analysis: A representative lot detected human tau oligomers formation in paraffin-embedded striatal sections of Huntington s diseased brains (Vuono, R., et al. (2015). Brain. 138(Pt 7):1907-1918).
Immunohistochemistry Analysis: A representative lot detected increased human tau P301L mutant oligomers formation in CA3 region of Tg4510 mice following FKBP51-expressing AAV viarl particles injection using 4% paraformaldehyde-fixed free-floating brain sections (Blair, L.J., et al. (2013). J. Clin. Invest. 123(10):4158-4169).
Immunofluorescence Analysis: A representative lot detected granule cell layer (GCL) neurons containing oligomers of virally expressed human P301L mutant tau 1 441 by fluorescent immunohistochemistry staining of brain sections from mice received recombinant viral injection to the medial entorhinal cortex (MEC) (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
Immunofluorescence Analysis: A representative lot detected greatly enhanced tau oligomers co-localized with that of oxidative nucleic acid damage marker 8-OH(d)G in human AD brain, as well as heat stress- (HS-) induced Tau oligomers formation in the brain CA1 region of THY-Tau22 transgenic mice expressing human tau with G272V and P301S mutation by fluorescent immunohistochemistry staining of paraffin-embedded brain tissue sections (Violet, M., et al. (2015). Neurobiol. Dis. 82:540-551).
Western Blotting Analysis: A representative lot detected human P301S tau oligomers-containing exosomal fractions from PS19 transgenic mice. Dietary supplementation with CSF-1R Inhibitor PLX3397 reduced exosomal tau oligomer accumulation (Asai, H., et al. (2015). Nat. Neurosci. 18(11):1584-1593).
The unpurified antiserum (Cat. No. ABN454) is also available for dot blot, ELISA, immunofluorescence, immunohistochemistry, immunoprecipitation, neutralization, and Western blotting applications.
Quality
Evaluated by Dot Blot analysis of recombinant human tau.
Dot Blot Analysis: 2 µg/mL of this antibody detected 100 ng of in vitro generated recombinant human tau oligomers, but not tau monomer.
Dot Blot Analysis: 2 µg/mL of this antibody detected 100 ng of in vitro generated recombinant human tau oligomers, but not tau monomer.
Target description
Variable depending on the size(s) of the oligomer(s). Uncharacterized bands may be observed in some lysate(s).
Physical form
Affinity purified.
Purified rabbit polyclonal antibody in PBS without preservatives.
Storage and Stability
Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Other Notes
Concentration: Please refer to lot specific datasheet.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
recommended
Product No.
Description
Pricing
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Acta neuropathologica communications, 7(1), 192-192 (2019-12-05)
Tau is a microtubule-binding protein that can receive various post-translational modifications (PTMs) including phosphorylation, methylation, acetylation, glycosylation, nitration, sumoylation and truncation. Hyperphosphorylation of tau is linked to its aggregation and the formation of neurofibrillary tangles (NFTs), which are a hallmark
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service