MABN827
Anti-Tau Antibody, clone T49 (Not human)
clone T49, from mouse
Synonym(s):
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau
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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
T49, monoclonal
species reactivity
mouse, rat, bovine
should not react with
human
technique(s)
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) , Mapt(281296)
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. Clone T49 exhibits immunoreactivity against bovine, rat, and murine, but not human, Tau (UniProt P29172, P19332, P10637, P10636, respectively).
Immunogen
Purified corresponding to bovine Tau.
Application
Anti-Tau Antibody, clone T49 (Not human) is an antibody against Tau for use in Western Blotting and Immunohistochemistry.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected Tau in mouse cerebral cortex, mouse kidney, and mouse small intestine tissue.
Western Blotting Analysis: A representative lot detected Tau in PS19 neurons treated with PBS or transduced with strain A or strain B FL a-syn pffs (Guo, J.L., et al. (2013). Cell. 154:103-117).
Western Blotting Analysis: A representative lot detected Tau in PS19 neurons treated with PBS or transduced with strain A or strain B FL a-syn pffs (Guo, J.L., et al. (2013). Cell. 154:103-117).
Quality
Evaluated by Western Blotting in mouse and human brain tissue lysate.
Western Blotting Analysis: 0.5 µg/mL of this antibody detected Tau in 10 µg of mouse and human brain tissue lysate.
Western Blotting Analysis: 0.5 µg/mL of this antibody detected Tau in 10 µg of mouse and human brain tissue lysate.
Target description
~53 kDa observed. This protein has multiple isoforms which range from 45-76 kDa
Physical form
Format: Purified
Other Notes
Concentration: Please refer to lot specific datasheet.
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Storage Class Code
12 - Non Combustible Liquids
WGK
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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Sheng Chen et al.
Nature communications, 15(1), 2436-2436 (2024-03-19)
Parkinson's disease (PD) is closely linked to α-synuclein (α-syn) misfolding and accumulation in Lewy bodies. The PDZ serine protease HTRA1 degrades fibrillar tau, which is associated with Alzheimer's disease, and inactivating mutations to mitochondrial HTRA2 are implicated in PD. Here
Antigoni Katsikoudi et al.
The Journal of biological chemistry, 295(37), 13079-13093 (2020-07-24)
Tau aggregation and hyperphosphorylation is a key neuropathological hallmark of Alzheimer's disease (AD), and the temporospatial spread of Tau observed during clinical manifestation suggests that Tau pathology may spread along the axonal network and propagate between synaptically connected neurons. Here
Michael Fassler et al.
Cells, 12(11) (2023-06-10)
TREM2 is a membrane receptor expressed on microglia that plays a pivotal role in the organization and function of these innate immune cell components within the neurodegenerated brain. Whereas TREM2 deletion has been studied extensively in experimental beta-amyloid and Tau-based
Elena Ficulle et al.
Scientific reports, 12(1), 2673-2673 (2022-02-19)
Cellular models recapitulating features of tauopathies are useful tools to investigate the causes and consequences of tau aggregation and the identification of novel treatments. We seeded rat primary cortical neurons with tau isolated from Alzheimer's disease brains to induce a
Sarah Helena Nies et al.
The Journal of biological chemistry, 297(4), 101159-101159 (2021-09-05)
In Alzheimer's disease (AD), deposition of pathological tau and amyloid-β (Aβ) drive synaptic loss and cognitive decline. The injection of misfolded tau aggregates extracted from human AD brains drives templated spreading of tau pathology within WT mouse brain. Here, we
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