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Biotin anti-Tau, 6-18 Antibody

Pricing & Availability
Clone
Tau 12 (See other available formats)
Regulatory Status
RUO
Other Names
PHF-tau, paired helical filament-tau, neurofibrillary tangle protein, microtubule-associated protein tau, isoform 4, G protein beta1/gamma2 subunit-interacting factor 1, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND
Isotype
Mouse IgG1
Ave. Rating
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Product Citations
publications
Tau-12_Biotin_Tau-6-18_Antibody_1_121219
IHC staining Biotin anti-Tau, 6-18 antibody (clone Tau 12) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using Sodium Citrate H.I.E.R., the tissue was incubated with 1.0 µg/mL of the primary antibody overnight at 4°C, followed by incubation with Alexa Fluor® 594 streptavidin (Cat. No. 405240) for one hour at room temperature. Nuclei were counterstained with DAPI. The image was captured with a 60X objective. Scale bar: 50 µm
  • Tau-12_Biotin_Tau-6-18_Antibody_1_121219
    IHC staining Biotin anti-Tau, 6-18 antibody (clone Tau 12) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using Sodium Citrate H.I.E.R., the tissue was incubated with 1.0 µg/mL of the primary antibody overnight at 4°C, followed by incubation with Alexa Fluor® 594 streptavidin (Cat. No. 405240) for one hour at room temperature. Nuclei were counterstained with DAPI. The image was captured with a 60X objective. Scale bar: 50 µm
  • Tau-12_Biotin_Tau-6-18_Antibody_2_121219
    IHC staining Biotin anti-Tau, 6-18 antibody (clone Tau 12) on formalin-fixed paraffin-embedded Alzheimer’s disease brain tissue. Following antigen retrieval using Sodium Citrate H.I.E.R., the tissue was incubated with 1.0 µg/mL of the primary antibody overnight at 4°C, followed by incubation with Alexa Fluor® 594 streptavidin (Cat. No. 405240) for one hour at room temperature. Nuclei were counterstained with DAPI. The image was captured with a 60X objective. Scale bar: 50 µm
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806505 25 µg £94
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806506 100 µg £297
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Description

Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyper-phosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Six isoforms of tau are generated by alternative splicing of the MAPT gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain.  Tau isoforms are differentially expressed during development.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
Preparation
The antibody was purified by affinity chromatography and conjugated with biotin under optimal conditions.
Concentration
0.5 mg/mL
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C. Do not freeze.
Application

IHC-P - Quality tested
Recommended Usage

Each lot of this antibody is quality control tested by formalin-fixed paraffin-embedded immunohistochemical staining. For immunohistochemistry, a concentration range of 0.1 - 1.0 µg/mL is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is specific for an epitope that lies between amino acids 6-18 of human Tau.

Application References

(PubMed link indicates BioLegend citation)
  1. Irwin D, et al. 2012. Brain. 135(Pt 3):: 807. (IHC-P) PubMed
  2. Horowitz PM, et al. 2004. J Neurosci. 24(36):7895 (WB)
  3. Sengupta U, et al. 2017. Ann Clin Transl Neurol. 4(4):226. (WB) PubMed
  4. Meredith JE, et al. 2013. PLoS One. 7;8(10):e76523 (ELISA, WB) PubMed
  5. Song L, et al. 2015, Mol Neurodegener. 10:14 (ELISA, WB) PubMed
RRID
AB_2861079 (BioLegend Cat. No. 806505)
AB_2861080 (BioLegend Cat. No. 806506)

Antigen Details

Structure
Unmodified Tau isoforms have an apparent molecular weight ranging from 33-79 kD. Additional high and low molecular weight Tau species have been observed in brain tissues.
Distribution

Tissue distribution: Central nervous system, peripheral ganglia and nerves, kidney, skeletal, and heart muscle.
Cellular distribution: Cytoskeleton, nucleus, plasma membrane, and cytosol.

Function
Tau promotes microtubule assembly and stability. The short tau isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
Interaction
Tau interacts with: Sequestosome-1, Peptidyl-prolyl cis-trans isomerase FKBP4, Casein kinase I isoform delta, Serine/threonine-protein kinase Sgk1, Laforin, and alpha-synuclein.
Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
Tau
Antigen References

1. Meredith JE Jr, et al. 2013. PLoS One. 8(10): e76523. PubMed
2. Goodall CA, et al. 2006. J. Neurol. Neurosurg. Psychiatry 77(1): 89. PubMed
3. Wang Y, Mandelkow E. 2016. Nat. Rev. Neurosci. 17(1):5-21. PubMed

Gene ID
4137 View all products for this Gene ID
UniProt
View information about Tau 6-18 on UniProt.org

Related FAQs

How many biotin molecules are per antibody structure?
We don't routinely measure the number of biotins with our antibody products but the number of biotin molecules range from 3-6 molecules per antibody.
Go To Top Version: 1    Revision Date: 12/12/2019

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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This data display is provided for general comparisons between formats.
Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors.
If you need assistance with selecting the best format contact our expert technical support team.

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