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Anti-Tau, 15-25 Antibody (Previously Covance catalog# MMS-520R)

Pricing & Availability
Clone
TAU-13 (See other available formats)
Regulatory Status
RUO
Other Names
Microtubule-associated protein tau, PHF-tau, paired helical filament-tau, neurofibrillary tangle protein, microtubule-associated protein tau, isoform 4, G protein beta1/gamma2 subunit-interacting factor 1
Previously
Covance Catalog# MMS-520R
Isotype
Mouse IgG1, κ
Ave. Rating
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Product Citations
publications
Tau‐13_Ascites_Tau-15-25_Antibody_1_073018
Western blot of anti-Tau, 15-25 antibody (clone TAU-13). Lane 1: Molecular weight marker; Lane 2: 20 µg of human Alzheimer's disease brain lysate; Lane 3: 20 µg of normal human brain lysate. The blot was incubated with a 1:500 dilution of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • Tau‐13_Ascites_Tau-15-25_Antibody_1_073018
    Western blot of anti-Tau, 15-25 antibody (clone TAU-13). Lane 1: Molecular weight marker; Lane 2: 20 µg of human Alzheimer's disease brain lysate; Lane 3: 20 µg of normal human brain lysate. The blot was incubated with a 1:500 dilution of the primary antibody overnight at 4°C, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
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835201 500 µL 336€
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Description

Tau proteins are microtubule-associated protein (MAPs) which are abundant in neurons of the central nervous system, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes and elsewhere. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is active primarily in the distal portions of axons providing microtubule stabilization as well as flexibility. Pathologies and dementias of the nervous system such as Alzheimer's disease feature tau proteins that have become defective and no longer stabilize microtubules properly. As a result, tau forms aggregates with specific structural properties referred to as Paired Helical Filaments (PHFs) that are a characteristic of many different types of dementias, known as tauopathies. Tau has two primary ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in human brain tissue, and they are distinguished by the number of binding domains. Three isoforms have three binding domains and the remaining three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (for binding to the negatively-charged microtubule). Tau isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They also differ in either zero, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-binding regions at the C-terminus. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). Tau is also a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. Phosphorylation has been reported on approximately 30 of these sites in normal tau proteins. Mechanisms that drive tau lesion formation in the highly prevalent sporadic form of AD are not fully understood, but appear to involve abnormal post-translational modifications (PTMs) that influence tau function, stability, and aggregation propensity.

Product Details
Technical Data Sheet (pdf)

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Preparation
Ascites
Concentration
The concentration is not quantified as this product is sold as undiluted crude mouse ascites fluid. The concentration might vary from lot-to-lot and an estimated concentration would be 1-3 mg/ml.
Storage & Handling
Store at -20°C or below. Upon initial thawing, apportion into working aliquots and store at -20°C or below. Avoid repeated freeze-thaw cycles to prevent denaturing the antibody. Do not store in frost-free freezers.
Application

WB - Quality tested
IHC-Other - Reported in the literature, not verified in house
Recommended Usage

Each lot of this antibody is quality control tested by western blotting. For western blotting, a dilution range of 1:500-1:1000 is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

TAU-13 is a mouse monoclonal antibody that binds to human tau and is able to stain brain tissue early in Alzheimer’s disease. TAU-13 is specific for human tau; it does not react with bovine, murine or rat tau. Preliminary assignment of its epitope indicates that it maps to amino acid residues 15-25 on the longest isoform of human tau.

This antibody clone has been reported for use on IHC of 4% PFA-fixed free floating sections1.

Application References
  1. Bi M, et al. 2011. PLoS ONE. 6:12. (IHC-other)
  2. García-Sierra F, et al. 2003. J Alzheimers Dis. 5:65–77. (IHC-other)
Product Citations
  1. Bresinsky M, et al. 2022. ACS Pharmacol Transl Sci. 5:20. PubMed
  2. Hochmair J, et al. 2022. EMBO J. 41:e108882. PubMed
  3. Steuer EL, et al. 2022. J Neurosci. 42:4737. PubMed
  4. Zhong S, et al. 2023. Molecules. 28:. PubMed
  5. Han J, et al. 2021. Theranostics. 11:8855. PubMed
  6. Crotti A, et al. 2019. Sci Rep. 9:9477. PubMed
  7. Liu P, et al. 2019. Acta Neuropathol Commun. 7:111. PubMed
  8. Busche MA, et al. 2019. Nat Neurosci. 22:57. PubMed
  9. Pickett EK, et al. 2019. Cell Rep. 29:3592. PubMed
  10. Zhu B, et al. 2022. Mol Neurodegener. 17:58. PubMed
  11. McCreedy DA, et al. 2021. Front Cell Neurosci. 15:684792. PubMed
  12. Zhao X, et al. 2016. Nat Med. 22:1268-1276. PubMed
  13. Liu P, et al. 2020. Sci Rep. 10:3869. PubMed
  14. Rauch JN, et al. 2020. Nature. 580:381. PubMed
  15. Fu H, et al. 2016. PLoS One. 11: 0159463. PubMed
  16. Rasmussen J, et al. 2021. Brain Pathol. :e13018. PubMed
  17. Nogueras-Ortiz C, et al. 2014. Front Neurosci. 7:277. PubMed
RRID
AB_2565341 (BioLegend Cat. No. 835201)

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. Castillo-Carranza DL, et al. 2014. J Neurosci. 12:4260. (WB)
Gene ID
4137 View all products for this Gene ID
UniProt
View information about Tau 15-25 on UniProt.org

Related FAQs

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Go To Top Version: 6    Revision Date: 01/29/2020

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.
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