MABN471
Anti-Tau Antibody, PAD, clone TNT-1
clone TNT-1, from mouse
Synonym(s):
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, Tau
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All Photos(4)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
TNT-1, monoclonal
species reactivity
mouse, rat, human
technique(s)
ELISA: suitable
dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)
General description
Tau or Microtubule-associated protein tau (MAPT), also known as neurofibrillary tangle protein and paired helical filament-tau (PHF-tau), is a cytosolic protein that promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of axonal polarity in neurons. Tau binds to and is thought to function as a linker protein between axonal microtubules and neural plasma membrane components. There are multiple isoforms, and the short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. PAD is the phosphatase activating domain, and has been demonstrated to be involved in the inhibition of anterograde, kinesin-based fast axonal transport (FAT) by activating axonal protein phosphatase 1 (PP1) and glycogen synthase kinase 3 (GSK3), independent of microtubule binding. Defects in Tau are thought to be the cause of a number of neurodegenerative diseases, including frontotemporal dementia (FTD), pallido-ponto-nigral degeneration (PPND), Pick disease of the brain (PIDB), corticobasal degeneration (CBD), supranuclear palsy type 1 (PSNP1), Alzheimer disease, and Parkinson disease.
Immunogen
KLH-conjugated linear peptide corresponding to human Tau.
Application
Anti-Tau, PAD, clone TNT-1 detects levels of Tau proteins & has been published & validated for use in WB, IHC, IF & ELISA.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
Western Blot Analysis: 1 µg/mL from a representative lot detected Tau, PAD in 10 µg of human and mouse cortex tissue lysates.
Immunohistochemistry Analysis: A 1:2,000 dilution from a representative lot detected Tau, PAD in human Alzheimer′s brain tissue.
Immunohistochemistry Analysis: A representative lot from an independent laboratory detected Tau, PAD in normal and Alzheimer′s tissues from entorhinal cortex, hippocampus, inferior temporal gyrus, and superior gyrus of control (Kanaan, N. M., et al. (2011). J Neurosci. 31(27):9858-9868.).
ELISA Analysis: A representative lot from an independent laboratory detected Tau, PAD in recombinant Tau protein (Kanaan, N. M., et al. (2011). J Neurosci. 31(27):9858-9868.).
Immunohistochemistry Analysis: A 1:2,000 dilution from a representative lot detected Tau, PAD in human Alzheimer′s brain tissue.
Immunohistochemistry Analysis: A representative lot from an independent laboratory detected Tau, PAD in normal and Alzheimer′s tissues from entorhinal cortex, hippocampus, inferior temporal gyrus, and superior gyrus of control (Kanaan, N. M., et al. (2011). J Neurosci. 31(27):9858-9868.).
ELISA Analysis: A representative lot from an independent laboratory detected Tau, PAD in recombinant Tau protein (Kanaan, N. M., et al. (2011). J Neurosci. 31(27):9858-9868.).
Quality
Evaluated by Western Blot in rat cortex tissue lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected Tau, PAD in 10 µg of rat cortex tissue lysate.
Western Blot Analysis: 1 µg/mL of this antibody detected Tau, PAD in 10 µg of rat cortex tissue lysate.
Target description
~55 kDa observed. Many isoforms are known to exist between 35-80 kDa An uncharacterized band may be observed in some cell lysates.
Linkage
Replaces: MAB10417
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
rat cortex tissue lysate
rat cortex tissue lysate
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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
12 - Non Combustible Liquids
wgk_germany
WGK 1
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’.
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Yuki Fujita et al.
STAR protocols, 1(3), 100111-100111 (2020-12-31)
Microglia, the resident immune cells of the central nervous system, accumulate along axons and support neuronal survival during the early postnatal period. Although methods have been developed to isolate microglia or neurons, the procedures for co-culture of these cells can
Michael G Agadjanyan et al.
Molecular neurodegeneration, 12(1), 33-33 (2017-05-06)
The experience from clinical trials indicates that anti-Aβ immunotherapy could be effective in early/pre-clinical stages of AD, whereas at the late stages promoting the clearing of Aβ alone may be insufficient to halt the disease progression. At the same time
Hayk Davtyan et al.
Vaccine, 35(16), 2015-2024 (2017-03-23)
By the time clinical symptoms of Alzheimer's disease (AD) manifest in patients there is already substantial tau pathology in the brain. Recent evidence also suggests that tau pathology can become self-propagating, further accelerating disease progression. Over the last decade several
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