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36-017

Sigma-Aldrich

Anti-cleaved-Tau (Asp421) Antibody, clone C3

clone C3, Upstate®, from mouse

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

100

Forme d'anticorps

purified antibody

Type de produit anticorps

primary antibodies

Clone

C3, monoclonal

Espèces réactives

human, rat, mouse

Fabricant/nom de marque

Upstate®

Technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

Isotype

IgG1

Numéro d'accès NCBI

NM_005910.3
NM_016834.2
NM_016835.2
NM_016841.2

Numéro d'accès UniProt

P10636

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Spécificité

cleaved-Tau

Immunogène

Synthetic peptide corresponding to amino acids 412-421(CSSTGSIDMVD) of human Tau with a Cys at the N-terminal end

Application

Anti-cleaved-Tau (Asp421) Antibody, clone C3 is an antibody against cleaved-Tau (Asp421) for use in IP, WB, IH.

Qualité

routinely evaluated by immunoblot on Tau fusion protein cleaved by Caspase 3 (Catalog #14-264)

Description de la cible

50-70kDa

Forme physique

0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol
Format: Purified

Informations légales

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

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Tarif

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

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F Biundo et al.
Translational psychiatry, 7(8), e1198-e1198 (2017-08-09)
TAU mutations are genetically linked to fronto-temporal dementia (FTD) and hyper-phosphorylated aggregates of Tau form neurofibrillary tangles (NFTs) that constitute a pathological hallmark of Alzheimer disease (AD) and FTD. These observations indicate that Tau has a pivotal role in the
Urmi Sengupta et al.
Methods in molecular biology (Clifton, N.J.), 1779, 113-146 (2018-06-11)
An increasing number of studies have demonstrated the existence of multiple conformational entities of tau, as have been observed for prion protein. We have developed and optimized techniques to isolate and study oligomeric tau strains both in vitro and ex
Modeling tau polymerization in vitro: a review and synthesis.
Gamblin, T Chris, et al.
Biochemistry, 42, 15009-15017 (2003)
Franck R Petry et al.
Methods in molecular biology (Clifton, N.J.), 1523, 263-272 (2016-12-16)
In Alzheimer's disease and other tauopathies, tau displays several abnormal post-translation modifications such as hyperphosphorylation, truncation, conformation, and oligomerization. Mouse monoclonal antibodies have been raised against such tau modifications for research, diagnostic, and therapeutic purposes. However, many of these primary
Michelle A Utton et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 22(15), 6394-6400 (2002-08-02)
We demonstrate that the microtubule-associated protein tau, in the form of enhanced green fluorescent protein (EGFP) tau, is transported along axons of neurons in culture in the slow component of axonal transport with a speed comparable with that previously measured
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