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577801

Sigma-Aldrich

Anti-Tau Mouse mAb (TAU-5)

liquid, clone TAU-5, Calbiochem®

Synonim(y):

Anti-Tau antibody

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About This Item

Kod UNSPSC:
12352203
NACRES:
NA.43

pochodzenie biologiczne

mouse

Poziom jakości

forma przeciwciała

purified antibody

rodzaj przeciwciała

primary antibodies

klon

TAU-5, monoclonal

Postać

liquid

nie zawiera

preservative

reaktywność gatunkowa

mouse, human, sheep, rat

producent / nazwa handlowa

Calbiochem®

warunki przechowywania

OK to freeze
avoid repeated freeze/thaw cycles

izotyp

IgG1

Warunki transportu

wet ice

temp. przechowywania

−70°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)

Opis ogólny

Protein G purified mouse monoclonal antibody. Recognizes the ~45-68 kDa phosphorylated and unphosphorylated forms of tau.
Recognizes the ~45-68 kDa Tau protein.
This Anti-Tau Mouse mAb (TAU-5) is validated for use in Frozen Sections, Immunoblotting, Immunoprecipitation, Paraffin Sections for the detection of Tau.

Immunogen

Bovine
Epitope: within the central region
purified bovine microtubule-associated proteins

Zastosowanie

Frozen Sections (1-2 µg/ml)

Immunoblotting (1 µg/ml)

Immunoprecipitation (10 µg per 200-500 µg cell lysate)

Paraffin Sections (1-2 µg/ml, heat pre-treatment required)

Opakowanie

Please refer to vial label for lot-specific concentration.

Ostrzeżenie

Toxicity: Standard Handling (A)

Postać fizyczna

In PBS.

Rekonstytucja

Following initial thaw, aliquot and freeze (-70°C). Do not store diluted antibody without carrier protein if the concentration is <50 µg/ml.

Inne uwagi

Papasozomenos, S.C. and Shanavas, A., 2002. Proc. Natl. Acad. Sci. USA99, 1140.
Rapoport, M., eta al. 2002. Proc. Natl. Acad. Sci. USA99, 6364.
When used for formalin/paraffin embedded sections, staining is enhanced by boiling tissue sections in 10 mM citrate buffer, pH 6.0, for 10-20 min followed by cooling at room temperature for 20 min prior to antibody incubation. Alternate splicing of tau mRNA and differential phosphorylation contribute to the heterogeneity of tau. Does not cross-react with other MAPS of tubulin. Recognizes both native and phosphorylated forms of tau. Variables associated with assay conditions will dictate proper working dilution.

Informacje prawne

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

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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Ricardo Gargini et al.
Frontiers in aging neuroscience, 11, 231-231 (2019-09-26)
The analysis of global and comparative genomics between different diseases allows us to understand the key biological processes that explain the etiology of these pathologies. We have used this type of approach to evaluate the expression of several neurodegeneration-related genes
Weijiang Dong et al.
Journal of neuroscience research, 87(14), 3176-3185 (2009-05-28)
Tau function is regulated by phosphorylation, and abnormal tau phosphorylation in neurons is one of the key processes associated with development of Alzheimer's disease and other tauopathies. In this study we provide evidence that phospholipid transfer protein (PLTP), one of
Ram Fridlich et al.
Molecular & cellular proteomics : MCP, 8(6), 1206-1218 (2009-03-13)
Rod-derived cone viability factor (RdCVF) is produced by the Nxnl1 gene that codes for a second polypeptide, RdCVFL, by alternative splicing. Although the role of RdCVF in promoting cone survival has been described, the implication of RdCVFL, a putative thioredoxin
Michael Dumbacher et al.
Molecular neurodegeneration, 13(1), 50-50 (2018-09-28)
Neuronal Ca2+ dyshomeostasis and hyperactivity play a central role in Alzheimer's disease pathology and progression. Amyloid-beta together with non-genetic risk-factors of Alzheimer's disease contributes to increased Ca2+ influx and aberrant neuronal activity, which accelerates neurodegeneration in a feed-forward fashion. As
Marta Fernández-Nogales et al.
Brain pathology (Zurich, Switzerland), 27(3), 314-322 (2016-06-25)
Increased incidence of neuronal nuclear indentations is a well-known feature of the striatum of Huntington's disease (HD) brains and, in Alzheimer's disease (AD), neuronal nuclear indentations have recently been reported to correlate with neurotoxicity caused by improper cytoskeletal/nucleoskeletal coupling. Initial

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