ABN454
Anti-Tau (T22), oligomeric Antibody
serum, from rabbit
Synonym(s):
Microtubule-associated protein tau oligomer, Tau oligomer, PHF-tau oligomer, Paired helical filament-tau oligomer, Neurofibrillary tangle protein oligomer
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All Photos(3)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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biological source
rabbit
Quality Level
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
technique(s)
ELISA: suitable
dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
neutralization: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MAPT(4137)
Related Categories
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
Dot Blot (Specificity) Analysis: A 1:1,000 dilution from a representative lot detected oligomeric tau, but not monomeric tau or tau fibrils.
Immunohistochemistry Analysis: A 1:245-1,000 dilution from a representative lot detected tau oligomers in frontal cortices from Alzheimer′s Diseased (AD) and Lewy Body Diseased (LBD) patients (Courtesy of Prof. Rakez Kayed, University of Texas, Galveston).
Immunofluorescence Analysis: A representative lot detected oligomeric tau in chronic traumatic encephalopathy (CTE) brain tissue sections, while little or no tau oligomer immunoreactivity was seen in non-CTE human brain sections. The tau oligomer immunoreactivity colocalized with that of tau pThr231 with a cis conformation, but not tau pThr231 with a trans conformation, between pThr231 and Pro232 (Kondo, A., et al. (2015). Nature. 523(7561):431-436).
Immunofluorescence Analysis: A representative lot detected oligomeric tau immunoreactivity in paraffin-embedded frontal cortex sections from Alzheimer′s diseased (AD) brains (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected oligomeric tau in chronic traumatic encephalopathy (CTE) in Tau Aggregate lysate.
Western Blotting Analysis: Representative lots detected oligomeric tau, but not monomeric tau, or any other oligomeric and fibrillar proteins (Wu J.W., et al. (2013). J. Biol. Chem. 288(3):1856-1870; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Dot Blot Analysis: A representative lot detected tau oligomers, but not tau monomer or paired helical filaments (PHFs) (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
ELISA Analysis: Representative lots detected vitro formed tau oligomers as well as tau oligomers in PBS-soluble brain extracts from progressive supranuclear palsy (PSP) patients (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
ELISA Analysis: A representative lot showed selective reactivity toward oligomeric tau, while exhibiting greatly reduced immunoreactivity toward tau fibrils, and no reactivity toward monomeric tau, or other protein oligomers or fibrils (e.g., Aβ, α-synuclein, or islet amyloid polypeptide) (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunoprecipitation Analysis: Representative lots immunoprecipitated oligomeric tau from Alzheimer′s Diseased (AD), but not non-AD brains (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Neutralizing Analysis: Representative lots neutralized oligomeric tau toxicity to SH-SY5Y human neuroblastoma cells (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunohistochemistry Analysis: A representative lot detected oligomeric tau immunoreactivity in paraffin-embedded brain sections from progressive supranuclear palsy (PSP) patients (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunohistochemistry Analysis: A 1:245-1,000 dilution from a representative lot detected tau oligomers in frontal cortices from Alzheimer′s Diseased (AD) and Lewy Body Diseased (LBD) patients (Courtesy of Prof. Rakez Kayed, University of Texas, Galveston).
Immunofluorescence Analysis: A representative lot detected oligomeric tau in chronic traumatic encephalopathy (CTE) brain tissue sections, while little or no tau oligomer immunoreactivity was seen in non-CTE human brain sections. The tau oligomer immunoreactivity colocalized with that of tau pThr231 with a cis conformation, but not tau pThr231 with a trans conformation, between pThr231 and Pro232 (Kondo, A., et al. (2015). Nature. 523(7561):431-436).
Immunofluorescence Analysis: A representative lot detected oligomeric tau immunoreactivity in paraffin-embedded frontal cortex sections from Alzheimer′s diseased (AD) brains (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected oligomeric tau in chronic traumatic encephalopathy (CTE) in Tau Aggregate lysate.
Western Blotting Analysis: Representative lots detected oligomeric tau, but not monomeric tau, or any other oligomeric and fibrillar proteins (Wu J.W., et al. (2013). J. Biol. Chem. 288(3):1856-1870; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Dot Blot Analysis: A representative lot detected tau oligomers, but not tau monomer or paired helical filaments (PHFs) (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
ELISA Analysis: Representative lots detected vitro formed tau oligomers as well as tau oligomers in PBS-soluble brain extracts from progressive supranuclear palsy (PSP) patients (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
ELISA Analysis: A representative lot showed selective reactivity toward oligomeric tau, while exhibiting greatly reduced immunoreactivity toward tau fibrils, and no reactivity toward monomeric tau, or other protein oligomers or fibrils (e.g., Aβ, α-synuclein, or islet amyloid polypeptide) (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunoprecipitation Analysis: Representative lots immunoprecipitated oligomeric tau from Alzheimer′s Diseased (AD), but not non-AD brains (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Neutralizing Analysis: Representative lots neutralized oligomeric tau toxicity to SH-SY5Y human neuroblastoma cells (Lasagna-Reeves, C.A., et al. (2012). Sci. Rep. 2:700; Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Immunohistochemistry Analysis: A representative lot detected oligomeric tau immunoreactivity in paraffin-embedded brain sections from progressive supranuclear palsy (PSP) patients (Lasagna-Reeves, C. A., et al. (2012). FASEB J. 26(5):1946-1959).
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
This Anti-Tau (T22) antibody, oligomeric is validated for use in Dot Blot, ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Neutralization, and Western blotting.
Quality
Evaluated by Western Blotting in human brain tissue lysates.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected tau oligomers in Alzheimer′s diseased (AD), but not non-AD, human brain tissue lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected tau oligomers in Alzheimer′s diseased (AD), but not non-AD, human brain tissue lysate.
Target description
Variable depending on the size(s) of the oligomer(s).
Physical form
Rabbit polyclonal serum containing 0.02% sodium azide.
Unpurified
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.
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.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
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’.
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Mahmoud B Maina et al.
Cells, 10(3) (2021-04-04)
The self-assembly of tau into paired helical filaments (PHFs) in neurofibrillary tangles (NFTs) is a significant event in Alzheimer's disease (AD) pathogenesis. Numerous post-translational modifications enhance or inhibit tau assembly into NFTs. Oxidative stress, which accompanies AD, induces multiple post-translational
Youssra K Al-Hilaly et al.
Journal of molecular biology, 429(23), 3650-3665 (2017-09-19)
Alzheimer's disease is characterized by the self-assembly of tau and amyloid β proteins into oligomers and fibrils. Tau protein assembles into paired helical filaments (PHFs) that constitute the neurofibrillary tangles observed in neuronal cell bodies in individuals with Alzheimer's disease.
Yang Yu et al.
Anesthesiology, 133(3), 595-610 (2020-07-24)
Sevoflurane anesthesia induces Tau phosphorylation and cognitive impairment in neonatal but not in adult mice. This study tested the hypothesis that differences in brain Tau amounts and in the activity of mitochondria-adenosine triphosphate (ATP)-Nuak1-Tau cascade between the neonatal and adult
Ron Balczon et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(9), e21807-e21807 (2021-08-13)
Pneumonia causes short- and long-term cognitive dysfunction in a high proportion of patients, although the mechanism(s) responsible for this effect are unknown. Here, we tested the hypothesis that pneumonia-elicited cytotoxic amyloid and tau variants: (1) are present in the circulation
Urmi Sengupta et al.
Annals of clinical and translational neurology, 4(4), 226-235 (2017-04-07)
With an increasing incidence of Alzheimer's disease (AD) and neurodegenerative tauopathies, there is an urgent need to develop reliable biomarkers for the diagnosis and monitoring of the disease, such as the recently discovered toxic tau oligomers. Here, we aimed to
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