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05-803

Sigma-Aldrich

Anti-Tau (3-repeat isoform RD3) Antibody, clone 8E6/C11

culture supernatant, clone 8E6/C11, Upstate®

Synonym(s):

G protein beta1/gamma2 subunit-interacting factor 1, Neurofibrillary tangle protein, Paired helical filament-tau, microtubule-associated protein tau, microtubule-associated protein tau, isoform 4.

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About This Item

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

biological source

mouse

Quality Level

antibody form

culture supernatant

antibody product type

primary antibodies

clone

8E6/C11, monoclonal

species reactivity

human

manufacturer/tradename

Upstate®

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MAPT(4137)

General description

Microtubule Associated Proteins, or MAPS, bind to the tubulin subunits of microtubule structures and regulate their functional stability. In the cell MAPs bind to monomer and multimerized tubulin. MAP binding to multimerized tubulin further stabilizes the formation of higher order microtubulin structures. MAP binding to microtubule structures is mediated through phosphorylation through Microtubule Affinity Regulated Kinase (MARK). Phosphorylation releases MAPs bound to microtubules, destabilizing the structure, driving it toward disassembly. There are predominately two MAP types, I, II. Type II MAP includes MAP2, MAP4, and tau and are found in nervous tissue. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains.

Specificity

Cross-reactivity with mouse and bovine expected due to sequence homology.
Recognizes Tau (3-repeat isoform RD3), Mr 45-65 kDa. Higher MW bands (68-72 kDa) represent phosphorylated Tau.

Immunogen

Bovine thyroglobulin conjugated synthetic peptide corresponding to amino acids 209-224 (KHQPGGGKVQIVYKPV) of human Tau (isoform RD3). In other isoforms of huTau this sequence spans amino acids 267-316, omitting the second repeat domain where it bridges RD1 and RD3. The immunizing sequence is identical in human, mouse and bovine.

Application

Anti-Tau (3-repeat isoform RD3) Antibody, clone 8E6/C11 is an antibody against Tau (3-repeat isoform RD3) for use in IH & WB.
Immunohistochemistry:
This antibody has been reported by an independent laboratory to detect Tau (3-repeat isoform RD3) in autoclaved paraffin brain sections (de Silva, R., 2003).

Differential Detection of Tauopathies:
(Togo, T., 2002.)
Research Category
Neuroscience
Research Sub Category
Neurotransmitters & Receptors

Neurodegenerative Diseases

Quality

Routinely evaluated by western blot on rat brain cytosol fraction.

Western Blot Analysis:
A 1:1000-1:4000 dilution of this lot detected Tau (3-repeat isoform RD3) in lysates from rat brain cytosol fraction.

Target description

~45-65 kDa; phosphorylated forms at 68-72 kDa

Physical form

Mouse culture supernatant containing 0.05% sodium azide. Frozen at -20°C.
Unpurified

Storage and Stability

Stable for 1 year at -20°C from date of receipt.
For maximum recovery of product, centrifuge the vial prior to removing the cap.

Handling Recommendations:
Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variabillity in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.

Analysis Note

Control
Lysates from rat brain cytosol fraction.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

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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Expression of the embryonal isoform (0N/3R) of the microtubule-associated protein tau in the adult rat central nervous system.
Torsten Bullmann,Wolfgang Hartig,Max Holzer,Thomas Arendt
The Journal of Comparative Neurology null
Differential involvement and heterogeneous phosphorylation of tau isoforms in progressive supranuclear palsy.
Gibb, G M, et al.
Brain Research Molecular Brain Research, 121, 95-101 (2004)
Marion Hogg et al.
Acta neuropathologica, 106(4), 323-336 (2003-07-29)
We report a case of rapidly progressive frontotemporal dementia presenting at age 33 years. At autopsy there was severe atrophy of the frontal and temporal lobes. Tau-positive Pick bodies, which ultrastructurally were composed of straight filaments, were present, accompanied by
Pamela McMillan et al.
The Journal of comparative neurology, 511(6), 788-803 (2008-10-18)
Tau is a microtubule-associated protein implicated in neurodegenerative tauopathies. Alternative splicing of the tau gene (MAPT) generates six tau isoforms, distinguishable by the exclusion or inclusion of a repeat region of exon 10, which are referred to as 3-repeat (3R)
Jennifer L Ziskin et al.
Acta neuropathologica communications, 3, 43-43 (2015-07-15)
Transthyretin/TTR gene mutations usually cause systemic amyloidotic diseases. Few TTR variants preferentially affect the central nervous system, manifesting as oculoleptomeningeal amyloidosis. Patients with TTR meningovascular amyloidosis often show dementia, however the neuropathologic features of dementia in these cases have not

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