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Purified anti-Tau, 404-441 Antibody (Previously Covance catalog# SIG-39423)

Pricing & Availability
Clone
Tau46 (See other available formats)
Regulatory Status
RUO
Other Names
Microtubule-associated protein tau, PHF-tau, paired helical filament-tau, neurofibrillary tangle, microtubule-associated protein tau, isoform 4, G protein beta1/gamma2 subunit-interacting factor 1, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND
Previously
Signet Catalog# 9423-02
Signet Catalog# 9423-05
Signet Catalog# 9423-10
Covance Catalog# SIG-39423
Isotype
Mouse IgG1, κ
Ave. Rating
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Product Citations
publications
Tau46_Purified_Tau404-441_Antibody_1_101718
Western blot of purified anti-Tau, 404-441 antibody (clone Tau46). Lane 1: Molecular weight marker; Lane 2: 20 µg of human Alzheimer's disease brain lysate; Lane 3: 0.1 µg of recombinant tau ladder. The blot was incubated with 1 µg/mL of the primary antibody for 60 minutes at room temperature, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • Tau46_Purified_Tau404-441_Antibody_1_101718
    Western blot of purified anti-Tau, 404-441 antibody (clone Tau46). Lane 1: Molecular weight marker; Lane 2: 20 µg of human Alzheimer's disease brain lysate; Lane 3: 0.1 µg of recombinant tau ladder. The blot was incubated with 1 µg/mL of the primary antibody for 60 minutes at room temperature, followed by incubation with HRP labeled goat anti-mouse IgG (Cat. No. 405306). Enhanced chemiluminescence was used as the detection system.
  • Tau46_Purified_Tau404-441_Antibody_2_101718
    IHC staining of purified anti-Tau, 404-441 antibody (clone Tau46) 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 60 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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806604 50 µL 90€
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806601 200 µL 300€
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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

Product Details

Verified Reactivity
Human
Antibody Type
Monoclonal
Host Species
Mouse
Formulation
Phosphate-buffered solution (no preservatives or carrier proteins).
Preparation
The antibody was purified by affinity chromatography.
Concentration
0.5 mg/mL
Storage & Handling
This antibody should be handled aseptically as it is free of preservatives such as Sodium Azide. Store this antibody 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 the vial label or CoA to find the proper storage conditions.
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, a concentration range of 1.0 - 10 µg/mL is suggested. It is recommended that the reagent be titrated for optimal performance for each application.

Application Notes

This antibody is effective in immunoblotting (WB), immunohistochemistry on formalin-fixed paraffin-embedded tissue (IHC-P).

This antibody is reactive to the amino acid sequence 404-441 of human Tau.

Application References

(PubMed link indicates BioLegend citation)
  1. Halford RW and Russell DW. 2009. Proc Natl Acad Sci U S A. 106:3502-6. (WB)
  2. Hoffmann R, et al. 1997. Biochemistry. 36(26):8114-24.
  3. Bramblett GT, et al. 1993. Neuron. 10(6):1089-99.
  4. Bramblett GT, et al. 1992. Lab Invest. 66(2):212-22.
  5. Kosik KS, et al. 1988. Neuron 1(9):817-25.
Product Citations
  1. Lo Cascio F, et al. 2020. J Biol Chem. 295:14807. PubMed
RRID
AB_2564709 (BioLegend Cat. No. 806604)
AB_2564709 (BioLegend Cat. No. 806601)

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
Specificity (DOES NOT SHOW ON TDS):
Tau 404-441
Specificity Alt (DOES NOT SHOW ON TDS):
Tau, 404-441
App Abbreviation (DOES NOT SHOW ON TDS):
WB,IHC-P
UniProt
View information about Tau 404-441 on UniProt.org
Go To Top Version: 6    Revision Date: 07.09.2024

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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