T1032-70
Clone Type
PolyclonalHost
RabbitSource
HumanIsotype
IgGGrade
Affinity PurifiedApplications
WBCrossreactivity
HuShipping Temp
Blue IceStorage Temp
-20°CRabbit Anti-Tau, phosphorylated (Ser404) (Tau Protein, Microtubule-associated Protein, MAP)
Tau is a neuronal microtubule-associated protein found predominantly on axons that functions 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’s disease (AD) brain. Hyperphosphorylated tau is also found in neurofibrillary lesions in a range of other central nervous system disorders. Hyperphosphorylation impairs the microtubule binding function of tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II, phosphorylate tau. Serine 404 is phosphorylated by GSK-3beta and cdk5 in vitro and in vivo.
Applications
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution
Western Blot 1:1000 Optimal dilutions to be determined by the researcher.
Positive Control
Recombinant human tau treated with GSK-3beta.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic phosphopeptide derived from a region of human tau that contains serine 404. The sequence is conserved in mouse and rat.
Form
Supplied as a liquid in PBS (without Mg2+ and Ca2+), 1mg/ml BSA (IgG, protease free), pH 7.2, 0.09% sodium azide, 50% glycerol. Also available wthout azide, BSA, glycerol. See T1032-70A.
Purity
Purified from by epitope-affinity chromatography.
Specificity
Recognizes human tau. Species sequence homology: Mouse and rat 100%.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
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 (cites the use of 44-732, 44-734, 44-736, 44-738, 44-740, 44-742, 44-744, 44-746, 44-750, 44-752, 44-758, 44-758 and 44-760).||2. Jenkins, S.M., et al. (2000) Modulation of tau phosphorylation and intracellular localization by cellular stress. Biochem. J. 345(Pt 2):263-270.||3. Mandelkow, E. (1999) Alzheimer's disease. The tangled tale of tau. Nature 402(6762):588-589. Goedert, M. (1999) Alzheimer's disease. Pinning down phosphorylated tau. Nature. 399(6738):739- 740.||4. Davis, P.K. and G.V. Johnson (1999) The microtubule binding of Tau and high molecular weight tau in apoptotic PC12 cells is impaired because of altered phosphorylation. J. Biol. Chem. 274(50):35686-35692.||5. 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.||6. Wang, J.Z., et al. (1998) Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase FEBS Lett. 436(1):28-34.USBio References
No references available