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Merck

36-017

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

clone C3, Upstate®, from mouse

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About This Item

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

biological source

mouse

Quality Level

100

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

NCBI accession no.

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

UniProt accession no.

P10636

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

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

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

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

Physical form

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

Analysis Note

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

Legal Information

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

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Lydia Reinhardt et al.
Neurobiology of disease, 182, 106126-106126 (2023-04-23)
Intraneuronal aggregates of the microtubule binding protein Tau are a hallmark of different neurodegenerative diseases including Alzheimer's disease (AD). In these aggregates, Tau is modified by posttranslational modifications such as phosphorylation as well as by proteolytic cleavage. Here we identify
View All Related Papers

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Global Trade Item Number

SKUGTIN
36-01704053252275302

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