Recombinant Human Tau, 306-311 Mutant, Protein, CF

Product Discontinued

Recombinant Human Tau, 306-311 Mutant, 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
  amino acids 306-311 (VQIVYK) are deleted
• Accession #: P10636-8
• Protein/Peptide Type: Recombinant Proteins
• Purity: >85%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 45 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: 2.3 mg/ml (50 μM) in PBS pH 7.4
• Purity: >85%, 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, 306-311 Mutant, 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--this 441 amino acid isoform is known as "2N4R," "Isoform Tau-F," "Tau-4" or "Tau 441" and is referenced in UniProt as P10636-8.  Amino acids 306-311 (VQIVYK) are missing in this deletion mutant.  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

Bioinformatics

• Uniprot:
  • P10636-8()