anti
PHFThis rabbit polyclonal antibody is raised against a preparation of PHF from a young Alzheimer patient. This antibody detects normal and pathological epitopes of tau proteins. It does not recognize MAP2 (Delacourte A, et al. Pathological proteins Tau 64 and 69 are specifically expressed in the somatodendritic domain of the degenerating cortical neurons during Alzheimer's disease. Demonstration with a panel of antibodies against Tau proteins. Acta Neuropathol (Berl). 1990;80(2):111-7.).
Saturated with a brain homogenate from a control, our antibody only recognizes pathological epitopes. With this approach, we have been able to demonstrate the specific profile of tau in progressive supranuclear palsy (Flament S, et al. Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol (Berl). 1991;81(6):591-6).
For animal models, we suggest to absorb the antisera with a brain homogenate from an animal control (a young one, if studies are devoted to aging)
Source:
A New Zealand rabbit was immunized sub-cutaneously with the PHF preparation.
Applications:
This antibody can be used for immunohistochemistry and western blotting.
Specificity:
1. Western-blot : in homogenates from brain of AD patients, this antibody mostly recognizes the characteristic triplet of Alzheimer's disease. Saturated, it detects the double of PSP and CBD.
2. Immunohistochemistry : this antibody recognizes neurofibrillary tangles, neuritic plaques and dystrophic neurites on frozen sections of Alzheimer's disease cortical brain tissue.
Presentation:
This rabbit polyclonal antibody to human Tau proteins is in 50% glycerol. There is no other additive or preservative. It is a total serum.
Instructions for use:
1. For Western-blot, a final dilution of 1/500 in TBS-Tween buffer.
2. For immunohistochemistry, use the antibody at a final dilution of 1/400 (in Coons buffer) for immunostaining on frozen sections of cortical brain tissue.
Note: The recommended concentrations are approximative values. For each application, a dose response assay should be performed to determine the optimal concentration for use.
FOR RESEARCH USE ONLY
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References:
Persuy P, et al. [See Related Articles] Anti-PHF antibodies: an immunohistochemical marker of the lesions of the Alzheimer's disease. Characterization and comparison with Bodian's silver impregnation. Virchows Arch A Pathol Anat Histopathol. 1985;407(1):13-23. PMID: 2409667; UI: 85246197.
Flament S, et al. [See Related Articles] Abnormal tau species are produced during Alzheimer's disease neurodegenerating process. FEBS Lett. 1989 Apr 24;247(2):213-6. PMID: 2497028; UI: 89232121.
Flament S, et al. [See Related Articles] [Direct demonstration of abnormal phosphorylation of Tau microtubular proteins in Alzheimer's disease]. C R Acad Sci III. 1989;308(3):77-82. French. PMID: 2493316; UI: 89150983.
Parent M, et al. [See Related Articles] [Alzheimer's disease: study of the distribution of tau proteins constituting helical filament pairs in human central nervous tissue]. C R Acad Sci III. 1988;306(13):391-7. French. PMID: 3136867; UI: 88310474.
Defossez A, et al. [See Related Articles] Alzheimer's disease: a new evidence for common epitopes between microtubule associated protein Tau and paired helical filaments (PHF): demonstration at the electron microscope level by a double immunogold labelling. Virchows Arch A Pathol Anat Histopathol. 1988;413(2):141-5. PMID: 2455379; UI: 88265833.
Defossez A, et al. Transformation of degenerating neurofibrils into amyloid substance in Alzheimer's disease: histochemical and immunohistochemical studies. J Neurol Sci. 1987 Oct;81(1):1-10. PMID: 2445923; UI: 88061420.
Defossez A, et al. [Immunocytochemical study at the ultrastructural level of neurofibrillary degeneration in Alzheimer's disease]. C R Acad Sci III. 1987;304(9):217-22. French. PMID: 3102001; UI: 87130207.
Delacourte A, et al. [See Related Articles] Observation of morphological relationships between angiopathic blood vessels and degenerative neurites in Alzheimer's disease. Virchows Arch A Pathol Anat Histopathol. 1987;411(3):199-204. PMID: 2441514; UI: 87293848.
Delacourte A, et al. Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments. J Neurol Sci. 1986 Dec;76(2-3):173-86. PMID: 3098926; UI: 87085674.
Defossez A, et al. [Immunohistochemical study of the basic lesions of Alzheimer's disease]. Encephale. 1986 Jul-Aug;12(4):161-8. French. PMID: 3539580; UI: 87080180.
Delacourte A, et al. [See Related Articles] [Biochemical characterization of an immune serum which specifically marks neurons in neurofibrillary degeneration in Alzheimer's disease]. C R Acad Sci III.
Flament S, et al. Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol (Berl). 1991;81(6):591-6. PMID: 1831952; UI: 91353193.
Flament S, et al. Tau marker? Nature. 1990 Jul 5;346(6279):22. PMID: 2114549; UI: 90309965.
Flament S, et al. Phosphorylation of Tau proteins: a major event during the process of neurofibrillary degeneration. A comparative study between Alzheimer's disease and Down's syndrome. Brain Res. 1990 May 14;516(1):15-9. PMID: 2142011; UI: 90304554.
Delacourte A, et al. [Towards the development of an in vivo study model of Alzheimer-type neurofibrillary degeneration]. Presse Med. 1990 Feb 3;19(4):170-3. French. PMID: 2137602; UI: 90160211.1986;303(11):439-44. French. PMID: 3096503; UI: 87050935.
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