577801
Anti-Tau Mouse mAb (TAU-5)
liquid, clone TAU-5, Calbiochem®
Synonym(s):
Anti-Tau antibody
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
TAU-5, monoclonal
form
liquid
does not contain
preservative
species reactivity
mouse, human, sheep, rat
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG1
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
unmodified
Gene Information
human ... MAPT(4137)
mouse ... Mapt(17762)
rat ... Mapt(29477)
General description
Protein G purified mouse monoclonal antibody. Recognizes the ~45-68 kDa phosphorylated and unphosphorylated forms of tau.
Recognizes the ~45-68 kDa Tau protein.
This Anti-Tau Mouse mAb (TAU-5) is validated for use in Frozen Sections, Immunoblotting, Immunoprecipitation, Paraffin Sections for the detection of Tau.
Immunogen
Bovine
Epitope: within the central region
purified bovine microtubule-associated proteins
Application
Frozen Sections (1-2 µg/ml)
Immunoblotting (1 µg/ml)
Immunoprecipitation (10 µg per 200-500 µg cell lysate)
Paraffin Sections (1-2 µg/ml, heat pre-treatment required)
Immunoblotting (1 µg/ml)
Immunoprecipitation (10 µg per 200-500 µg cell lysate)
Paraffin Sections (1-2 µg/ml, heat pre-treatment required)
Packaging
Please refer to vial label for lot-specific concentration.
Warning
Toxicity: Standard Handling (A)
Physical form
In PBS.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C). Do not store diluted antibody without carrier protein if the concentration is <50 µg/ml.
Other Notes
Papasozomenos, S.C. and Shanavas, A., 2002. Proc. Natl. Acad. Sci. USA99, 1140.
Rapoport, M., eta al. 2002. Proc. Natl. Acad. Sci. USA99, 6364.
Rapoport, M., eta al. 2002. Proc. Natl. Acad. Sci. USA99, 6364.
When used for formalin/paraffin embedded sections, staining is enhanced by boiling tissue sections in 10 mM citrate buffer, pH 6.0, for 10-20 min followed by cooling at room temperature for 20 min prior to antibody incubation. Alternate splicing of tau mRNA and differential phosphorylation contribute to the heterogeneity of tau. Does not cross-react with other MAPS of tubulin. Recognizes both native and phosphorylated forms of tau. Variables associated with assay conditions will dictate proper working dilution.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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Weijiang Dong et al.
Journal of neuroscience research, 87(14), 3176-3185 (2009-05-28)
Tau function is regulated by phosphorylation, and abnormal tau phosphorylation in neurons is one of the key processes associated with development of Alzheimer's disease and other tauopathies. In this study we provide evidence that phospholipid transfer protein (PLTP), one of
Ram Fridlich et al.
Molecular & cellular proteomics : MCP, 8(6), 1206-1218 (2009-03-13)
Rod-derived cone viability factor (RdCVF) is produced by the Nxnl1 gene that codes for a second polypeptide, RdCVFL, by alternative splicing. Although the role of RdCVF in promoting cone survival has been described, the implication of RdCVFL, a putative thioredoxin
Michael Dumbacher et al.
Molecular neurodegeneration, 13(1), 50-50 (2018-09-28)
Neuronal Ca2+ dyshomeostasis and hyperactivity play a central role in Alzheimer's disease pathology and progression. Amyloid-beta together with non-genetic risk-factors of Alzheimer's disease contributes to increased Ca2+ influx and aberrant neuronal activity, which accelerates neurodegeneration in a feed-forward fashion. As
Ricardo Gargini et al.
Frontiers in aging neuroscience, 11, 231-231 (2019-09-26)
The analysis of global and comparative genomics between different diseases allows us to understand the key biological processes that explain the etiology of these pathologies. We have used this type of approach to evaluate the expression of several neurodegeneration-related genes
Marta Fernández-Nogales et al.
Brain pathology (Zurich, Switzerland), 27(3), 314-322 (2016-06-25)
Increased incidence of neuronal nuclear indentations is a well-known feature of the striatum of Huntington's disease (HD) brains and, in Alzheimer's disease (AD), neuronal nuclear indentations have recently been reported to correlate with neurotoxicity caused by improper cytoskeletal/nucleoskeletal coupling. Initial
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