
Thermo Fisher Scientific Phospho-Tau (Thr205) Polyclonal Antibody
Rabbit polyclonal antibody recognizing phospho-Tau (Thr205); ideal for Western blot and ELISA; detects hyperphosphorylated Tau relevant to Alzheimer’s research; lyophilized form, reconstitutable to 0.5 mg/mL; for research use only.
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Applications
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 0.5–2 µg/mL |
| ELISA | 0.05–0.2 µg/mL |
Product Specifications
| Property | Description |
|---|---|
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | Synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding phospho-threonine 205 of human tau |
| Conjugate | Unconjugated |
| Form | Lyophilized |
| Storage Conditions | -20°C or -80°C if preferred |
| Shipping Conditions | Wet ice |
Product Specific Information
Reconstitute the lyophilized powder with deionized water (or equivalent) to a final concentration of 0.5 mg/mL.
Tau is a microtubule-associated phosphoprotein (MAP) localized in neuronal axons. It promotes tubulin polymerization and stabilizes microtubules. Tau proteins constitute a family of six isoforms, ranging from 352 to 441 amino acids. These isoforms differ by the presence of three or four repeat regions in the C-terminal part and one or two inserts in the N-terminal portion.
Tau is hyperphosphorylated by ERK, GSK-3, TPKII, and CDK5. At least thirty phosphorylation sites have been described, including Thr205. Phosphorylation at these sites reduces tau’s ability to promote microtubule assembly. Hyperphosphorylated tau is the major protein of paired helical filaments (PHFs), which form neurofibrillary tangles in Alzheimer’s disease and other CNS disorders.
This antibody was developed in rabbit using a synthetic phosphopeptide (KLH-coupled) corresponding to residues surrounding threonine 205 of human tau.
Target Information
Tau is a neuronal microtubule-associated protein found predominantly on axons. Its primary function is to promote tubulin polymerization and stabilize microtubules. The C-terminus binds axonal microtubules, while the N-terminus binds neural plasma membrane components, acting as a linker between both structures.
In its hyperphosphorylated form, Tau is the major component of paired helical filaments (PHF), the building blocks of neurofibrillary lesions in Alzheimer’s disease. Hyperphosphorylation impairs Tau’s microtubule-binding function, leading to destabilization and neuronal degeneration. Tau phosphorylation is mediated by kinases such as GSK-3β, PKA, CDK5, and casein kinase II.
Hyperphosphorylated Tau is found in neurofibrillary lesions associated with Alzheimer’s disease, Pick’s disease, frontotemporal dementia, corticobasal degeneration, and progressive supranuclear palsy.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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