Description: Recombinant full-length human tag-free Tau-383 was expressed in E. coli cells.

Storage, Stability, and Shipping: Store product at –70^oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Applications: Kinase Assay, Western Blot

Molecular Weight: ~52 kDa

Gene Aliases: Tau-D, (N0R4), MAPT, MSTD; PPND; DDPAC; MAPTL; MTBT1; MTBT2; FTDP-17; FLJ31424; MGC138549

Scientific Background: Tau-383 or Tau-D is a member of the Tau family of proteins which function to stabilize the microtubules by binding to them. Tau proteins are subject to phosphorylation and this phenomenon regulates the association of the Tau protein with the microtubules (1). Deposits of Alzheimer's disease AD-associated proteins, such as hyperphosphorylated Tau, as well as other shared misfolded proteins, such as, β-amyloid precursor protein (βAPP), ubiquitin, and various chaperones and protein kinases are thought to play a pathologic role in the cognitive decline and muscular failure. Malfunctioning of Tau proteins is associated with microtubules disintegration and collapsing of the neuronal transport system (2).

References: 
1. Zilka, N., et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 2006; 508: 3582-3588.

2. Rial, A. et al: Calcium Dyshomeostasis in β-Amyloid and Tau-bearing Skeletal Myotubes. J. Biol. Chem., 2004; 279: 3524-53532.

		Purity:  Sample Purity Data. For specific information on a given lot, see related technical data sheet.

		Tau Proteins:  The image of seven Tau proteins, from left to right: Tau-441, Tau-410, Tau-412, Tau-381, Tau-383, Tau-352 and Tau-316.

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