C13, N15 Tau-441, Uniformly Labeled

Tau is a family of six isoforms, derived from a single gene by alternative mRNA splicing. They vary in size from 352 to 441 amino acids (36.8 to 45.9 kDa) and differ from one another in having three or four microtubule binding repeats (R) of 31-32 amino acids each, and two, one or none amino terminal inserts (N) of 29 amino acids each. Tau promotes the assembly and maintains the structure of microtubules in neuronal cells. While the fetal brain contains a single isoform of tau (Tau-352) the adult brain has several isoforms. Tau is both phosphorylated and O-GlcNAcylated6. The normal brain tau contains 2-3 moles of phosphate/mole of the protein. In Alzheimer disease tau is hyperphosphorylated, containing 3-4-fold more phosphate/mole of the protein than the normal tau and is the major protein subunit of paired helical filaments (PHF) that form the neurofibrillary tangles (NFT). NFT accumulation correlates with the clinical progression of Alzheimer’s disease.

Catalog ID: T-1103

$1,615.00$2,699.00

  • Product Details

    • Physical State: White lyophilized powder
    • Temperature Storage: -20°C
    • Temperature Shipping: Ambient
    • Sequence:
      MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEDVTAPLV DEGAPGKQAA AQPHTEIPEG TTAEEAGIGD TPSLEDEAAG HVTQARMVSK SKDGTGSDDK KAKGADGKTK IATPRGAAPP GQKGQANATR IPAKTPPAPK TPPSSGEPPK SGDRSGYSSP GSPGTPGSRS RTPSLPTPPT REPKKVAVVR TPPKSPSSAK SRLQTAPVPM PDLKNVKSKI GSTENLKHQP GGGKVQIINK KLDLSNVQSK CGSKDNIKHV PGGGSVQIVY KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQGL
    • Source: Recombinant. A DNA sequence encoding the human tau-441 (2N4R isoform) sequence was expressed in E. coli with N15 as the nitrogen source and C13 as the carbon source. No his-tag.
    • Purity: >90% by SDS-PAGE
    • Molecular Mass: 48,400 Da theoretical
  • References

    1. Avila, J., et al., (2004) Physiol Rev., 84 : 361
    2. Goedert, M., (1993) Trends Neurosci., 16 : 460
    3. Mandelkow, E., et al., (1996) Ann N Y Acad Sci., 777 : 96
    4. Goedert, M., et al., (1989) Neuron., 3 : 519
    5. Himmler, et al., (1989) Mol Cell Biol., 9 : 1381
    6. Tai, C., et al., (2020) Neuron., 106(3) : 421-437.e11
    7. Nobuhara, C., et al., (2017) Am J Pathol., 187(6) : 1399–1412