Recombinant Human Tau Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Tau Protein, CF Summary

Details of Functionality
Concentrations for in vitro assays will depend on experimental conditions and detection methods.
Source
E. coli-derived human Tau protein
Accession #
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

Theoretical MW
46 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer
X mg/ml (X μM) in PBS pH 7.4
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Tau Protein, CF

  • DDPAC
  • FLJ31424
  • FTDP-17
  • G protein beta1/gamma2 subunit-interacting factor 1
  • MAPT
  • MGC138549
  • microtubule-associated protein tau
  • MSTD
  • MSTDMAPTL
  • MTBT1
  • MTBT1Neurofibrillary tangle protein
  • MTBT2
  • Neurofibrillary tangle protein
  • PHF-tau
  • PPND
  • Tau
  • TAUPaired helical filament-tau

Background

Tau is a microtubule-associated protein expressed primarily in neurons.  Carboxy-terminal domains of Tau associate with and stabilize microtubule structure, while other domains bind to the plasma membrane.  Abnormal Tau phosphorylation may result in the self-assembly of tangles of paired helical and/or straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other neurodegenerative diseases.  Properly folded Tau is highly soluble, but when the protein becomes misfolded it forms insoluble aggregates that can damage cytoplasmic functions, interfere with axonal transport and ultimately lead to cell death.  This recombinant protein is untagged.
  1. Billingsley M.L. & Kincaid R.L. (1997)  Biochem. J.  323: 577
  2. Bloom G.S. (2014) JAMA Neurol.  71: 505
  3. Cripps D. et al. (2006) J. Biol. Chem.  281: 10825
  4. Harada A. et al (1994)  Nature  369: 488
  5. Lei P. et al. (2010)  Int. J. Biochem. Cell Biol.  42: 1775
 

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Blogs on Tau.

The C99 fragment of amyloid precursor protein (APP)
Alzheimer’s Disease (AD) is a neurodegenerative disorder that is characterized by an abundance of the beta-amyloid peptide in the brain.  When AD was first discovered, it was determined that beta-amyloid was produced as a result of the prote...  Read full blog post.

Tau - A microtubule associated protein as a biomarker for Alzheimer's disease
The tau protein is a microtubule associated protein found mostly in neuronal cells where it regulates the stability of axonal microtubules as well as kinesin-dependent transport. Tau is relevant in the study of various neurological disorders as ab...  Read full blog post.

PINK1: All work and no fun
The protein PINK1 is a mitochondrial-located serine/threonine kinase (PTK) that maintains organelle function and integrity. It not only protects organelles from cellular stress, but it also uses the selective auto-phagocytosis process for cleaning and...  Read full blog post.

Using Amyloid beta peptides in Alzheimer's Disease Immunization
Amyloid beta (AB) peptide has a central role in the neurodegeneration of Alzheimer's disease (AD). Immunization of AD transgenic mice with AB-42 peptide reduces both the spatial memory impairments and AD-like neuropathologic changes.Therapeutic im...  Read full blog post.

New Study Links Tau Mutations to Microglial Immune Response
Tau proteins are abundant in the axons of neurons in the central nervous system (CNS), and play a key role in microtubule formation and stabilization. Antibody studies have identified six tau isoforms, all produced by alternative mRNA splicing of the...  Read full blog post.

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Bioinformatics

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