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Tau (human) polyclonal antibody (TAUY9)

BML-TA3119-0100 100 µl 429.00 USD
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Product Details

Alternative Name:Microtubule-associated protein Tau
Immunogen:Synthetic peptide corresponding to aa 12-27 (E12DHAGTpYGLGDRKDQG27) of human tau isoform 6 (2N4R) phosphorylated at Tyr18.
UniProt ID:P10636
Source:Purified from rabbit serum.
Species reactivity:Human
Applications:IHC (FS), WB
Recommended Dilutions/Conditions:Immunohistochemistry (formalin-fixed tissue section, use of high temperature antigen retrieval technique may be required)
Western Blot (1:3000)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Blocking Peptide:For Blocking peptide see Prod. No. BML-TP9119.
Formulation:Liquid. In PBS, pH 7.2, containing 0.1% sodium azide.
Handling:Store unopened vial at -20°C until required for use. Avoid repeated freeze-thaw cycles.
Shipping:Blue Ice
Long Term Storage:-20°C
Scientific Background:Tau is the principal microtubule-associated protein located in axons in the nervous system where it participates in events including the elongation, stabilisation and bundling of microtubules. The tau family consists of six isoforms identified by the insertion of three or four partial repeats of 30-31 amino acids in the C-terminal region. Subcellular fractionation studies have revealed tau to be associated with the membrane fraction, as well as with the cytoskeletal fraction and there is some evidence that the N-terminal domain of tau may be responsible for membrane binding as well as interaction with other cellular components. Tau extracted from human fetal and neonatal brains is moderately phosphorylated with 5-9 phosphorylated serine/threonine residues per molecule. Normal adult human brain tau shows a marked reduction in phosphorylation, but in certain neurodegenerative diseases (tauopathies) tau becomes hyperphosphorylated (6-15 phosphates per tau molecule have been identified) and associates to form filamentous aggregates. In Alzheimer’s disease (AD) hyperphosphorylated tau polymerises to form a mixture of paired helical filaments (PHF) and straight filaments which accumulate and contribute to the formation of neurofibrillary tangles - one of the characteristic features of AD. It was reported in 1998 that tau could be tyrosine phosphorylated when co-transfected with the src-family protein tyrosine kinase fyn. In 2004 the same group, using phospho-specific antibodies, reported that fyn phosphorylated Tyr18 of brain tau at an early developmental stage in mice, but that tyrosine phosphorylated tau was undetectable in adult mice. However, they also showed that PHF preparations were reactive to the tau-pTyr18-specific antibodies, implicating a role for fyn – and possibly other tyrosine kinases - in the neurodegenerative process.
Regulatory Status:RUO - Research Use Only
Tau (human) polyclonal antibody (TAUY9) Western blot
Western blot analysis of human tau (2N4R) using various antisera. Lane 1: MW markers; Lanes 2 and 3: Tau1 (control); Lanes 2, 4 and 6: unphosphorylated tau; lanes 3, 5 and 7: p56lck phosphorylated tau; ~400ng tau per lane. Lanes 4 and 5: antiphosphotyrosine (4G10) (1:1000); Lanes 6 and 7: antiserum TA 3119 (1:3000). Enhanced chemiluminescence (1 min exposure). Image courtesy of Professor Brian Anderton (Institute of Psychiatry, London, U.K.)
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Tau (human) polyclonal antibody (TAUY9) Western blot

Product Literature References

Neuronal uptake and propagation of a rare phosphorylated high-molecular-weight tau derived from Alzheimer’s disease brain: S. Takeda, et al.; Nat. Commun. 6, 8490 (2015), Application(s): Immunocytochemistry, Abstract;
Rapid tyrosine phosphorylation of neuronal proteins including tau and focal adhesion kinase in response to amyloid-beta peptide exposure: Involvement of src family protein kinases: R. Williamson, et al.; J. Neurosci. 22, 10 (2002), Abstract; Full Text
Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system: M. Goedert, et al.; PNAS 89, 1983 (1992), Abstract; Full Text
Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: Identification as the microtubule-associated protein tau: M. Goedert, et al.; PNAS 85, 4051 (1988), Abstract; Full Text

General Literature References

Phosphorylation of tau by fyn: implications for Alzheimer's disease: G. Lee, et al.; J. Neurosci. 24, 2304 (2004), Abstract; Full Text
Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments: T. Maas, et al.; J. Biol. Chem. 275, 15733 (2000), Abstract; Full Text
Tau protein isoforms, phosphorylation and role in neurodegenerative disorders: L. Buée, et al.; Brain Res. Brain Res. Rev. 33, 95 (2000), (Review), Abstract;
Tau interacts with src-family non-receptor tyrosine kinases: G. Lee, et al.; J. Cell Sci. 111, 3167 (1998), Abstract; Full Text
Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain: R. Brandt, et al.; J. Cell Biol. 131, 1327 (1995), Abstract; Full Text
Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease: E. Köpke, et al.; J. Biol. Chem. 268, 24374 (1993), Abstract; Full Text
The extent of phosphorylation of fetal tau is comparable to that of PHF-tau from Alzheimer paired helical filaments: A. Kenessey, et al.; Brain Res. 629, 40 (1993), Abstract;
Molecular characterization of microtubule-associated proteins tau and MAP2: M. Goedert, et al.; Trends Neurosci. 14, 193 (1991), (Review), Abstract;

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