T7194
Anti-phospho-Tau (pThr231) antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution
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About This Item
Prodotti consigliati
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
affinity isolated antibody
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Stato
buffered aqueous glycerol solution
Reattività contro le specie
mouse, rat, human
tecniche
western blot: 1:1,000 using recombinant human tau treated with GSK-3β
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
modifica post-traduzionali bersaglio
phosphorylation (pThr231)
Informazioni sul gene
human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)
Specificità
Peptide competition studies demonstrate the specificity of the antibody – only the phosphopeptide immunogen blocks the antibody signal.
Immunogeno
chemically synthesized phosphopeptide derived from the region of human tau that contains threonine231.
Applicazioni
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
Stato fisico
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.
Esclusione di responsabilità
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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Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°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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