Tau, phosphorylated (Ser396) (Tau Protein, Microtubule-associated Protein, MAP)

Tau is a neuronal microtubule-associated protein found predominantly on axons. The function of tau is to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer

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SPECIFICATIONS

Catalog Number

T1032-66

Size

10 Blots

Applications

WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a liquid in PBS (without Mg2+ and Ca2+), 1mg/ml BSA (IgG, protease free), pH 7.3, 0.05% sodium azide, 50% glycerol. Also available without azide, BSA. See T1032-66A.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Liu, F., et al. (2002) Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. FEBS Letters 530(1-3):209-214. 2. Liu, F., et al. (2002) Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease. FEBS Lett. 512(1-3):101-106.. 3. Savage, M.J., et al. (2002) Activation of c-Jun N-terminal kinase and p38 in an Alzheimer's disease model is associated with amyloid deposition. J. Neurosci. 22(9):3376-3385. 4. Alonso, A.D., et al. (2001) Interaction of tau isoforms with Alzheimer's disease abnormally hyperphosphorylated tau and in vitro phosphorylation into the disease-like protein. J. Biol. Chem. 276(41):37967-37973. 5. Mandelkow, E. (1999) Alzheimer's disease. The tangled tale of tau. Nature 402(6762):588-589. 6. Jensen, P.H., et al. (1999) alpha-synuclein binds to tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 396. J. Biol. Chem. 274(36):25481-25489. 7. Sontag, E., et al. (1999) Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies. J. Biol. Chem. 274(36):25490-25498.

Additional Info

Recognizes human tau.