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Recombinant Human Tau 412 (1N4R) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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Recombinant Human Tau 412 (1N4R) 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
Met1 - Leu412
Accession #
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
43 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.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a solution in PBS.
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 412 (1N4R) 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.  There are multiple forms of Tau. The product is a 412 amino acid isoform known as "1N4R," "Isoform Tau-E" or "Tau 412" and is also referenced in UniProt as P10636-7.  
  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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