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Merck
CN

36-017

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

clone C3, Upstate®, from mouse

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
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产品名称

Anti-cleaved-Tau (Asp421) Antibody, clone C3, clone C3, Upstate®, from mouse

Quality Level

biological source

mouse

antibody form

purified antibody

antibody product type

primary antibodies

clone

C3, monoclonal

species reactivity

human, rat, mouse

manufacturer/tradename

Upstate®

technique(s)

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

isotype

IgG1

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

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

Analysis Note

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

Application

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

Biochem/physiol Actions

cleaved-Tau

General description

50-70kDa

Immunogen

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

Physical form

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

Legal Information

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

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存储类别

10 - Combustible liquids

wgk

WGK 1


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Modeling tau polymerization in vitro: a review and synthesis.
Gamblin, T Chris, et al.
Biochemistry, 42, 15009-15017 (2003)
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
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
Argyrophilic grain disease is a sporadic 4-repeat tauopathy
Togo, Takashi, et al
Journal of Neuropathology and Experimental Neurology, 61, 547-556 (2002)

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