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MABN827

Sigma-Aldrich

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

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

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).

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.

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


Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

MABN827:


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
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
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
Alberto Carpinteiro Soares et al.
The Journal of biological chemistry, 296, 100636-100636 (2021-04-09)
Tauopathies, such as Alzheimer's disease (AD), are neurodegenerative disorders characterized by the deposition of hyperphosphorylated tau aggregates. Proteopathic tau seeds spread through the brain in a temporospatial pattern, indicative of transsynaptic propagation. It is hypothesized that reducing the uptake of
Parissa Fereydouni-Forouzandeh et al.
Methods in molecular biology (Clifton, N.J.), 2754, 309-321 (2024-03-21)
Tau is a microtubule-associated protein enriched in the axonal compartment. Its most well-known function is to bind and stabilize microtubules. In Alzheimer's disease and other neurodegenerative diseases known as tauopathies, tau undergoes several abnormal post-translational modifications including hyperphosphorylation, conformational changes

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