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Merck

T7194

Sigma-Aldrich

Anti-phospho-Tau (pThr231) antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous glycerol solution

reactividad de especies

mouse, rat, human

técnicas

western blot: 1:1,000 using recombinant human tau treated with GSK-3β

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

phosphorylation (pThr231)

Información sobre el gen

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

Especificidad

Peptide competition studies demonstrate the specificity of the antibody – only the phosphopeptide immunogen blocks the antibody signal.

Inmunógeno

chemically synthesized phosphopeptide derived from the region of human tau that contains threonine231.

Aplicación

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Forma física

Solution in Dulbecco′s phosphate buffered saline (without Mg2+ and Ca2+), pH 7.3, containing 50% glycerol, 1.0 mg/mL BSA (IgG, protease free) and 0.05% sodium azide.

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Su Y Yim et al.
International journal of molecular medicine, 24(1), 91-96 (2009-06-11)
Selenium reportedly contribute to the modulation process of protein phosphorylation to regulate various cellular functions including growth, differentiation, proliferation and development. The aim of this study was to investigate whether selenium and Selenoprotein M (SelM) affects the mechanism of Alzheimer's
Eun-Bum Kang et al.
Journal of exercise nutrition & biochemistry, 19(3), 199-209 (2015-11-04)
Neurofibrillary tangles, one of pathological features of Alzheimer's disease, are produced by the hyperphosphorylation and aggregation of tau protein. This study aimed to investigate the effects of treadmill exercise on PI3K/AKT/mTOR signal transmission, autophagy, and cognitive ability that are involved
Young Ju Lee et al.
Molecular medicine reports, 7(5), 1571-1578 (2013-04-03)
Alzheimer's disease (AD) is closely associated with significant defects in glucose metabolism. To investigate whether AD pathology induced by overexpression of human mutant presenilin 2 (PS2) protein induces changes in glucose metabolism, glucose‑related factors were analyzed in the brain of
S M Jenkins et al.
The Biochemical journal, 345 Pt 2, 263-270 (2000-01-06)
Tau is a microtubule-associated protein that is functionally modulated by phosphorylation and hyperphosphorylated in several neurodegenerative diseases. Because phosphorylation regulates both normal and pathological tau functioning, it is of great interest to identify the signalling pathways and enzymes capable of

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