axolGEM iPSC-Derived Neural Stem Cells MAPT P301L HET

axolGEM iPSC-Derived Neural Stem Cells MAPT P301L HET (1.5 million cells) and Neural Plating-XF Medium (30 mL)

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Human iPSC-Derived Neural Stem Cells that have been genetically edited using CRISPR-Cas9 technology to introduce the P301L mutation (CCG>CTG) into the MAPT gene. This line is heterozygous for the P301L mutation where one allele contains the mutation and the other allele is wild type at the locus. Click on the product images to see the data and further details.

The P301L mutation MAPT has been implicated in frontotemporal dementia and parkinsonism (Dumanchin et al., 1998). The mutation affects only the 4R isoforms of MAPT since the exon containing the mutation is spliced out of 3R isoforms (Hutton et al., 1998). Aggregated MAPT/tau protein in affected patients consisted mainly of the 4R isoform (Hutton et al., 1998). The P301L mutation promotes aggregation of MAPT/tau protein into ordered paired helical filaments and beta sheet formation in vitro (von Bergen et al., 2001).

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Starting material Dermal fibroblast
Donor gender Female
Donor age at sampling 64 yrs
Karyotype Normal
Reprogramming method Episomal vector
Induction method Monolayer & chemically defined medium
Genetic modification Heterozygous for the MAPT P301L mutation (CCG>CTG)
Genetic modification Contains a puromycin resistance cassette (intronic)
Size ≥1.5 million cells
Kit components 1 vial of Neural Stem Cells (≥1.5 million cells) and 1 bottle of Neural Plating-XF Medium (30 mL)
Growth properties Adherent
Shipping conditions Dry ice
Storage conditions Liquid nitrogen
  • Read nowDumanchin C, Camuzat A, Campion D et al. Segregation of a missense mutation in the microtubule-associated protein tau gene with familial frontotemporal dementia and parkinsonism. Human Molecular Genetics (1998)
  • Read nowHutton M, Lendon CL, Rizzu P et al. Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17. Nature (1998)
  • Read nowvon Bergen M, Barghorn S, Li L et al. Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure. The Journal of Biological Chemistry (2001)