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Key Documents

05-348

Sigma-Aldrich

Anti-Tau Antibody, clone 5E2

clone 5E2, Upstate®, from mouse

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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

clone

5E2, monoclonal

species reactivity

bovine, rat, rabbit, mouse, human

manufacturer/tradename

Upstate®

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Specificity

several parts of Tau protein between 50kDa and 70kDa

Immunogen

Fetal heat stable MAPS

Application

Detect Tau using this Anti-Tau Antibody, clone 5E2 validated for use in WB, IH.
Research Category
Neuroscience
Research Sub Category
Apoptosis - Additional

Neurodegenerative Diseases

Quality

routinely evaluated in immunoblot on rat brain preparations

Target description

50-70kDa

Linkage

Replaces: MAB10417

Physical form

0.1M Tris-glycine, pH 7.4, containing and 0.05% sodium azide
Format: Purified
Protein G Chromatography

Storage and Stability

2 years at -20°C

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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.

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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MAP2 and tau segregate into dendritic and axonal domains after the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum.
Kosik, K S and Finch, E A
The Journal of Neuroscience, 7, 3142-3153 (1987)
W R Markesbery et al.
Neurobiology of aging, 14(4), 303-307 (1993-07-01)
Neuropil threads were quantitated in the neuropil (excluding senile plaques) of the superior frontal gyrus of 6 late stage patients with Alzheimer's disease (AD) and 6 age-matched control subjects using tau immunocytochemistry and computerized morphometric image analysis. The mean percent
N W Kowall et al.
Annals of neurology, 22(5), 639-643 (1987-11-01)
The microtubule-associated protein tau, a major antigenic component of paired helical filaments, has been demonstrated in neurofibrillary tangles and in neurites of senile plaques. With optimal fixation and histochemical methods, we show the normal axonal location of tau protein in
A C McKee et al.
Annals of neurology, 26(5), 652-659 (1989-11-01)
Cytoskeletal disruption is a key pathological feature of Alzheimer's disease (AD). We used refined immunocytochemical techniques to define the range of abnormalities affecting the microtubule system in AD hippocampus. Minimal tau and tubulin immunoreactivity was granular and accumulated in otherwise
Tau epitopes are incorporated into a range of lesions in Alzheimer's disease.
Joachim, C L, et al.
Journal of Neuropathology and Experimental Neurology, 46, 611-622 (1987)

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