36-017
Anti-cleaved-Tau (Asp421) Antibody, clone C3
clone C3, Upstate®, from mouse
Sign Into View Organizational & Contract Pricing
All Photos(1)
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
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.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)
Specificity
cleaved-Tau
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.
Quality
routinely evaluated by immunoblot on Tau fusion protein cleaved by Caspase 3 (Catalog #14-264)
Target description
50-70kDa
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
recommended
Product No.
Description
Pricing
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Modeling tau polymerization in vitro: a review and synthesis.
Gamblin, T Chris, et al.
Biochemistry, 42, 15009-15017 (2003)
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)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service