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Proteins and Peptides

Tau (K18) Delta K280 Mutant Pre-formed Fibrils

Product Sizes
100 ug
SPR-477-100UG
2 x 100 ug
SPR-477-2X100UG
5 x 100 ug
SPR-477-5X100UG
About this Product
SKU:
SPR-477
Additional Names:
Tau PFFs, Tau PFF, Tau protein Pre-formed Fibrils, Tau aggregates, microtubule-associated protein Tau, MAPT, MAP, microtubule-associated protein, Paired Helical Filament-Tau, Phf-Tau, Neurofibrillary Tangle Protein, G Protein Beta1/Gamma2 Subunit-Interacting Factor 1, Isoform 4, tubulin-associated unit, MAPT DeltaK280, D DeltaK280 Tau, K18 delta K280 Tau, truncated D DeltaK280 Tau
Application:
Cell-based/Functional Assay, SDS-PAGE, Western Blot
CE/IVD:
RUO
Concentration:
2 mg/ml
Extra Details:
Alzheimer's Disease (AD) is the most common neurodegenerative disease, affecting 10% of seniors over the age of 65 (1). It was named after Alois Alzheimer, a German scientist who discovered tangled bundles of fibrils where neurons had once been in the brain of a deceased patient in 1907 (2). Tau (tubulin-associated unit) is normally located in the axons of neurons where it stabilizes microtubules. Tauopathies such as AD are characterized by neurofibrillary tangles containing hyperphosphorylated tau fibrils (3). The D DeltaK280 mutation is associated with frontotemporal dementia and promotes fibrillization into paired helical filaments (PHFs) in the absence of heparin and other inducers (4). K18 is a truncated form of human tau containing only the 4 microtubule binding repeats (5).
Immunogen:
Tau (K18) Delta K280 Mutant
Molecular Weight:
~15 kDa
Purity:
>95%
Purification:
Ion Exchange
Sequence:
MSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRE
Shipping Conditions:
Dry Ice
Storage Conditions:
-70[o]C
Supplier:
StressMarq Biosciences
Type:
Proteins, Peptides, Small Molecules & Other Biomolecules: Recombinant Proteins
TEM of Human K18 K280 Deletion Tau Pre-formed Fibrils (PFFs) (SPR-477)
Thioflavin T is a fluorescent dye that binds to beta sheet-rich structures, such as those in tau fibrils. Upon binding, the emission spectrum of the dye experiences a red-shift and increased fluorescence intensity. Thioflavin T emission curves show increased fluorescence (correlated to tau aggregation) over time when tau monomers (SPR-476) are combined with tau fibrils (SPR-477).