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 PHF-tau Antibodies 

Specific antibodies for hyper-phosphorylated Tau (paired helical filament, PHF).

Thermo Scientific Human PHF Tau Antibodies

Thermo Scientific Pierce PHF-tau antibodies are specific for hyper-phosphorylated Tau. Anti-PHF-tau antibody clone AT8 has been used extensively to bind PHF-tau in neurofibrillary tangles in samples from Alzheimer's patients. It is extremely well-published for use in ELISA, immunohistochemistry, immunoblot, Western blot, and related applications. Clone AT8 recognizes Alzheimer tau in its native state of phosphorylation and does not bind the six human isoforms of unphosphorylated tau. (ref 2). It is specific for PHF-tau doubly phosphorylated at Ser202 and Thr205 (refs 2,11,26). It has also been shown to cross-react with Tau doubly phosphorylated at Ser199 / 202 and Ser205 / 208 (ref 26).

Anti-PHF-tau antibody clones AT180 and AT270 have also been used successfully to stain neurofibrillary tangles containing PHF-tau. Clone AT180 recognizes PHF-tau doubly-phosphorylated at Thr231 and Ser235 (refs 10,11). Clone AT270 recognizes PHF-tau phosphorylated at Thr181 (refs 10,11). Based on immunoblots, Thr-181 and Thr-231 are normal phosphorylation sites in immature and adult brain tau, but are more heavily phosphorylated in PHF tau (ref 10).

Clone AT100 recognizes PHF-tau phosphorylated at Ser212 and Thr214. When compared with antibody clones AT8, AT180, and AT270, it appeared to be the most specific for Alzheimer’s tau, with no recognition of normal fetal or adult biopsy tissue, though Alzheimer tau is more highly phosphorylated at the phosphoepitopes of antibody clones AT8, AT180, and AT270. (ref 34).

Anti-Tau antibody clone HT7 is often used alongside the PHF-tau antibodies to measure total human Tau in human samples or samples from transgenic rats and mice. (refs 5,6,15,20).

Product# Type Format Isotype Clone# Cross-Reactivity Applications
MN1020 Purified F, CF, PF Mouse IgG1 AT8 Tau doubly phosphorylated at Ser202/Thr205 (ref 2,11,26). Cross-reacts with tau phosphorylated at  Ser199/202 and Ser205/208 (ref 26).

ELISA (ref 21,26,31)
IF (ref 1,27,30)
IH (ref 3,4,5,6,14,15,27)
IH: paraffin
(ref 1,16-18,22,25,33)
WB (ref 1,2,5,10,11,12,
15,20,22,24,26,32,34)

MN1020B Biotin-labeled F, CF, PF Mouse IgG1 AT8 Same as above IF
WB
MN1040 Purified F, CF, PF Mouse IgG1/K AT180 Tau doubly phosphorylated at Thr231 and Ser235. (Weak recognition of phosphorylation at Thr231 only) (ref 10,11) IF (ref 7)
IH (ref 6,15)
WB (ref 5,7,10, 12,15,20,12,34)
MN1040B Biotin-labeled F, CF, PF Mouse IgG1/K AT180 Same as above IF
WB
MN1050 Purified F, CF, PF Mouse IgG1/K AT270 Tau phosphorylated at Thr181 (ref 10,11)

IF (ref 7)
IH (ref 5)
WB (ref 5,7,8,10,12,
15,20,28,32,34)

MN1060 Purified   Mouse IgG1/K AT100 Tau doubly phosphorylated at Ser212/Thr214. (ref 34) IH (ref 6,9,15)
WB (ref 5,7,21,34)
Format Abbreviations: F=frozen, L=lyophilized, C=carrier, CF=carrier-free, P=preservative, PF=preservative-free  

Related Neuroscience Products

References

  1. Arima, K., et al. (2000). NACP/alpha-synuclein and tau constitute two distinctive subsets of filaments in the same neuronal inclusions in brains from a family of parkinsonism and dementia with Lewy bodies: double-immunolabeling fluorescence and electron microscope studies. Acta Neuropathol. 100(2), 115-121.
  2. Biernat, J., et al. (1992). The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J. 11(4), 1593-1597.
  3. Braak, E., et al. (1994). A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol. 87, 554-567.
  4. Broe, M., et al. (2004). Astrocytic degeneration relates to the severaity of disease in frontotemporal dementia. Brain. 127(10), 2214-2220.
  5. Caccamo, A., et al. (2007). Lithium reduces tau phosphorylation but not Aβ or working memory deficits in a transgenic model with both plaques and tangles. Am. J. Pathol. 170(5), 1669-1675.
  6. Dawson, H.N., et al. (2007). The tau N279K exon 10 splicing mutation recapitulates frontotemporal dementia and parkinsonism linked to chromosome 17 tauopathy in a mouse model. J. Neurosci. 27(34), 9155-9168.
  7. DeTure, M., et al. (2002). Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau. Am. J. Pathol. 161(5), 1711-1722.
  8. Feijoo, C., et al. (2004). Evidence that phosphorylation of the microtubule-associated protein tau by SAPK4/p38δ at Thr50 promotes microtubule assembly. J. Cell Sci., 118, 397-408.
  9. Fratta, P. et al. (2005). Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and amyloid-β precursor protein-overexpressing cultured human muscle fibers. Am. J. Pathol. 167(2), 517-526.
  10. Goedert, M., et al. (1994). Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J., 301, 871-877.
  11. Goedert, M., et al. (1996). Tau protein and the neurofibrillary pathology of Alzheimer's disease. Ann. N. Y. Acad. Sci. 777: 121-131.
  12. Green, K.N., et al. (2007). Dietary docosahexaenoic acid and docosapentaenoic acid ameliorate amyloid-β and tau pathology via a mechanism involving presenilin 1 levels. J. Neurosci. 27(16), 4385-4395.
  13. Hoffmann, R., et al. (1997). Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry. 36(26), 8114-24.
  14. Hu, W.T., et al. (2006). Cognitive impairment and celiac disease. Arch. Neurol. 63, 1440-1446.
  15. Ittner, L.M., et al. (2008). Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. PNAS. 105(41), 15997-16002.
  16. Jicha, G.A., et al. (2006). Neuropathologic outcome of mild cognitive impairment following progression to clinical dementia. Arch. Neurol. 63, 674-681.
  17. Keegan, B.M., et al. (2008). Sporadic adult-onset leukoencephalopathywith neuroaxonal spheroids mimicking cerebral MS. Neurology. 70, 1128-1133.
  18. Klos, K.J. et al. (2008). Brain metal concentrations in chronic liver failure patientswith pallidal T1 MRI hyperintensity. Neurology. 67, 1984-1989.
  19. Kosik, K.S., et al. (1990). Tau protein and neurodegeneration. Mol. Neurobiol. 4(3-4), 171-179.
  20. Luo, W., et al. (2007) Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. PNAS, 104(22), 9511-9516.
  21. Mailliot, C., et al. (1998). Alzheimer-specific epitope of AT100 in transfected cell lines with tau: toward an efficient cell model of tau abnormal phosphorylation. Neurosci. Lett. 255, 13-16.
  22. Mercken, M., et al. (1992). Monoclonal antibodies with selective specificity for Alzheimer Tau are directed against phosphatase-sensitive epitopes. Acta Neuropathol. 84, 265-272.
  23. Mi, K., et al. (2006). The low density lipoprotein receptor-related protein 6 interacts with glycogen synthase kinase 3 and attenuates activity. J. Biol. Chem. 281(8), 4787-4794.
  24. Ohsawa, I., et al. (2008). Age-dependent neurodegeneration accompanying memory loss in transgenic mice defective in mitochondrial aldehyde dehydrogenase 2 activity. J. Neurosci. 28(24), 6239-6249.
  25. Petersen, R.C., et al. (2006). Neurophathalogic features of amnestic mild cognitive impairment. Arch. Neurol. 63, 665-672.
  26. Porzig, R., et al. (2007). Epitope mapping of mAbs AT8 and Tau5 directed against hyperphosphorylated regions of the human tau protein. Biochem. Biophys. Res. Commun. 358(2), 644-649.
  27. Schofield, E., et al. (2003). Severity of gliosis in Pick's disease and frontotemporal lobar degeneration: tau-positive glia differentiate these disorders. Brain. 126, 827-840.
  28. Shahani, N. et al. (2006). Tau aggregation and progressive neuronal degeneration in the absence of changes in spine density and morphology after targeted expression of Alzheimer's disease-relevant tau constructs in organotypic hippocampal slices. J. Neurosci. 26(22), 6103-6114.
  29. Spillantini, M. G., et al. (1996). Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles. Acta Neuropathol. 92(1), 42-48.
  30. Uchihara, T., et al. (2001). Evolution from pretangle neurons to neurofibrillary tangles monitored by thiazen red combined with Gallyas method and double immunofluorescence. Acta Neuropathol. 101(6), 535-539.
  31. Vandermeeren, M., et al. (1993). Detection of tau Proteins in normal and Alzheimer's disease cerebrospinal fluid with a sensitive sandwich enzyme-linked immunosorbent assay. J. Neurochem. 61, 1828-1834.
  32. Wen, Y., et al. (2008). Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3β mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing. J. Neurosci. 28(10), 2624-2632.
  33. Whitwell, J.L., et al. (2007). Rates of cerebral atrophy differ I different degenerative pathologies. Brain. 130, 1148-1158.
  34. Zheng-Fischhofer, Q., et al. (1997). Sequential phosphorylation of Tau by glycogen synthase kinase-3β and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur. J. Biochem. 252, 542-552.


Ordering Information
Bulk quantities: InquireBulk quantities: Inquire    Certificate of AnalysisCertificate of Analysis   Product InstructionsProduct Instructions   MSDSMSDS
Product # Description Pkg. Size Files Price
MN1020 Human PHF-tau MAb (clone AT8)
100 µg Certificate of Analysis MSDS for product # MN1020 Human PHF-tau MAb (clone AT8) $484.00

MN1020B Human PHF-tau Biotin-labeled MAb (clone AT8) 50 µg Certificate of Analysis MSDS for product # MN1020B Human PHF-tau Biotin-labeled MAb (clone AT8) $465.00

MN1040 Human PHF-tau MAb (clone AT180)
100 µg Certificate of Analysis MSDS for product # MN1040 Human PHF-tau MAb (clone AT180) $465.00

MN1040B Human PHF-tau Biotin-labeled MAb (clone AT180) 50 µg Certificate of Analysis MSDS for product # MN1040B Human PHF-tau Biotin-labeled MAb (clone AT180) $465.00

MN1050 Human PHF-tau MAb (clone AT270)
100 µg Certificate of Analysis MSDS for product # MN1050 Human PHF-tau MAb (clone AT270) $480.00

MN1060 Human PHF-tau MAb (clone AT100)
100 µg Certificate of Analysis MSDS for product # MN1060 Human PHF-tau MAb (clone AT100) $480.00


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