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| Cat. No. 314-0P |
100 µg protein, lyophilized. For reconstitution add 100 µl H2O to get a 1mg/ml solution in TBS. Then aliquot and store at -20°C to -80°C until use. Control proteins should be stored at +4°C when still lyophilized. Do not freeze! |
| Applications |
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| Immunogen | Recombinant protein corresponding to the N-terminal half of mouse Tau-D (UniProt Id: P10637-5) |
| Recommended dilution | Optimal concentrations should be determined by the end-user. |
| Matching antibodies | 314 002, 314 003, 314 004, 314 006, 314 011, 314 008, 314 308 |
| Remarks |
This control protein consists of the recombinant protein (aa 3 - 214 of mouse tau) that has been used for immunization. It has been tested in preadsorption experiments and blocks efficiently and specifically the corresponding signal in Western blots. The amount of protein needed for efficient blocking depends on the titer and on the affinity of the antibody to the antigen. |
| Data sheet | 314-0p.pdf |
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There are two major classes of heat-stable microtubule-associated proteins (MAPs): MAP2 and Tau (MAPT).
Tau is expressed in several isoforms in human brain (Tau-A, 2N4R/Tau-F, 1N4R/Tau-E, 0N4R/Tau-D, 2N3R/Tau-C, 1N3R/Tau-B, 0N3R) and rodents (Tau-A, 2N4R/Tau-F, 1N4R/Tau-E, 0N4R/Tau-D) (1). Tau helps to stabilize axonal microtubules and modulate axonal transport, with isoform diversity and phosphorylation status determining their dynamics and affinity for microtubules. Tauopathies, often associated with abnormal phosphorylation (2, 3), can be classified according to the Tau isoforms present in the pathological inclusions. For instance, Pick's disease (PiD) is characterized by tangles containing 3R-Tau isoforms (0N3R, 1N3R, and 2N3R), whereas 4R-Tau (0N4R, 1N4R, and 2N4R) accumulates in disorders like progressive supranuclear palsy (PSP) and corticobasal degeneration (CBD). In Alzheimer's disease (AD) aggregates consist of all Tau isoforms (1).
Tau is abundantly expressed in the central and peripheral nervous system. Compared to the CNS, the PNS shows a predominance of 4R Tau isoforms (0N4R, 1N4R, 2N4R), which are thought to provide stronger microtubule binding and stability needed for long peripheral axons (1, 4).
Since microtubule dynamics are central to cell division, migration, and morphology, aberrations in Tau expression have been implicated in several types of cancer (5). Notably, Tau is increasingly recognized for its role in tumor progression and resistance to cancer therapy, with glioblastoma (GBM), making Tau a potential biomarker and therapeutic target (6,7).