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Description
Human iPSC-Derived Neural Stem Cells that have been genetically edited using CRISPR-Cas9 technology to introduce the V337M mutation (GTG>ATG) in the MAPT gene. This line is heterozygous for the V337M mutation where 1 allele has the mutation and the other allele is wild type. Click on the product images to see the data and further details.
The V337M mutation in MAPT has been implicated in frontotemporal dementia and may have a role in Alzheimer's disease. The mutation leads to accelerated aggregation of MAPT/tau protein into filament structures (Nacharaju et al., 1999) and makes the MAPT/tau protein more susceptible to hyperphosphorylation (Alonso et al., 2004).
Product Specification
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 V337M mutation (GTG>ATG)
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)
Nacharaju P, Lewis J, Easson C, Yen S, Hackett J, Hutton M, Yen SH. Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. (1999)
Alonso Ad, Mederlyova A, Novak M, Grundke-Iqbal I, Iqbal K. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem. (2004)
Human iPSC-Derived Neural Stem Cells that have been genetically edited using CRISPR-Cas9 technology to introduce the V337M mutation (GTG>ATG) in the MAPT gene. This line is heterozygous for the V337M mutation where 1 allele has the mutation and the other allele is wild type. Click on the product images to see the data and further details.
The V337M mutation in MAPT has been implicated in frontotemporal dementia and may have a role in Alzheimer's disease. The mutation leads to accelerated aggregation of MAPT/tau protein into filament structures (Nacharaju et al., 1999) and makes the MAPT/tau protein more susceptible to hyperphosphorylation (Alonso et al., 2004).
Read nowNacharaju P, Lewis J, Easson C, Yen S, Hackett J, Hutton M, Yen SH. Accelerated filament formation from tau protein with specific FTDP-17 missense mutations. FEBS Lett. (1999)
Read nowAlonso Ad, Mederlyova A, Novak M, Grundke-Iqbal I, Iqbal K. Promotion of hyperphosphorylation by frontotemporal dementia tau mutations. J Biol Chem. (2004)
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