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Purified anti-Tau, 185-195 Antibody (Previously Covance catalog# MMS-5018)

Pricing & Availability
Clone
77E9 (See other available formats)
Regulatory Status
RUO
Other Names
Microtubule-associated protein tau, PHF-tau, Paired Helical Filament tau
Previously
Covance Catalog# MMS-5018
Isotype
Mouse IgG1, κ
Ave. Rating
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Product Citations
publications
77E9_Purified_Tau_185-195__Antibody_1_051718
Western blot of purified anti-Tau, 185-195 antibody (clone 77E9). Lane 1: Molecular weight marker; Lane 2: 5 µl of recombinant human Tau protein ladder; Lane 3: 20 µg of normal human brain lysate; Lane 4: 20 µg of human Alzheimer's disease brain lysate. The blot was incubated with 1 µg/mL 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.
  • 77E9_Purified_Tau_185-195__Antibody_1_051718
    Western blot of purified anti-Tau, 185-195 antibody (clone 77E9). Lane 1: Molecular weight marker; Lane 2: 5 µl of recombinant human Tau protein ladder; Lane 3: 20 µg of normal human brain lysate; Lane 4: 20 µg of human Alzheimer's disease brain lysate. The blot was incubated with 1 µg/mL 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.
  • 77E9_Purified_Tau_185-195__Antibody_2_051718
    IHC staining of purified anti-Tau, 185-195 antibody (clone 77E9) on formalin-fixed paraffin-embedded human Alzheimer's disease brain tissue. Following antigen retrieval using Sodium Citrate H.I.E.R., the tissue was incubated with 1 µg/ml of the primary antibody for 20 minutes at room temperature. BioLegend´s Ultra-Streptavidin (USA) HRP kit (Multi-Species, DAB, Cat. No. 929901) was used for detection followed by hematoxylin counterstaining, according to the protocol provided. The image was captured with a 40X objective. Scale bar: 50 µm
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814402 25 µL £77
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814401 100 µL £189
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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
Immunogen
This monoclonal antibody was raised against full-length human tau.
Formulation
Phosphate-buffered solution.
Preparation
The antibody was purified by affinity chromatography.
Concentration
1 mg/ml
Storage & Handling
The antibody solution should be stored undiluted between 2°C and 8°C. Please note the storage condition for this antibody has been changed from -20°C to between 2°C and 8°C. You can also check your vial or your CoA to find the most accurate storage condition for this antibody.
Application

WB - Quality tested
IHC-P - Verified
Recommended Usage

Each lot of this antibody is quality control tested by Western blotting. For Western blotting, the suggested use of this reagent is 1.0 - 10 µg per ml. For immunohistochemistry on formalin-fixed paraffin-embedded tissue sections, a concentration range of 0.5 - 1.0 µg/ml is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

BioLegend is the Exclusive Provider of this Antibody Product

Product Citations
  1. Vos A, et al. 2015. Alzheimers Dement. 11: 1461-1469. PubMed
RRID
AB_2715845 (BioLegend Cat. No. 814402)
AB_2564783 (BioLegend Cat. No. 814401)

Antigen Details

Biology Area
Cell Biology, Neurodegeneration, Neuroscience, Protein Misfolding and Aggregation
Molecular Family
Tau
Gene ID
4137 View all products for this Gene ID
UniProt
View information about Tau on UniProt.org

Related FAQs

There are no FAQs for this product.
Go To Top Version: 5    Revision Date: 10/03/2019

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.
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