Mouse anti-Microtubule-associated protein (Tau) Antibody
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Product Description
Specifications
| Size | 20 µg, 100 µg, 200 µg, 500 µg |
| Estimated Lead Time | 1-2 business days |
| Specificity | The antibody specifically detected the Tau protein derived from human brain tissue in both ELISA and WB. This antibody showed no cross-reactivity with other unrelated protein. |
| Accession Number | NP_058518 |
| Immunogen | Immunogen was recombinant protein derived from human Tau. This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with the immunogen. The IgG fraction of tissue culture supernatant was purified by Protein G/A affinity chromatography. |
| Recommended Applications | ELISA (recommended work dilution= 1:1, 000-4, 000), Western Blotting( recommended work dilution= 2-5 µg/ml), Note: Other applications are not tested yet. Optimal dilutions should be determined by each laboratory for each application. |
| Reconstitution | Supplied as lyophilized and purified antibody originally containing PBS, without Preservative Stabilizers, such as Sodium Azide. The final concentration is indicated on the shipping vial. The antibody is stable for at least years from the data of receipt when stored at -20°C to -70°C. Reconstituted antibody (recommended with H20 1 mg/ml) can also be aliquoted and stored frozen at -20°C to -70°C in a manual defrost freezer for months without detectable loss activity. Upon reconstitution, the antibody can be stored at 4°C for 1 month. Please avoid freeze-thaw cycles. |
| Research Area | Cytoskeletal Reorganization |
| Shipping Type | Ambient temperature |
| Storage | -20°C |
Description
Microtubule-associated protein, tau is abnormally hyperphosphorylated in the brain of patients with Alzheimer's disease, and is the major protein subunit of paired helical filaments. There is also a significant pool of non-paired helical filament abnormally phosphorylated tau in Alzheimer's disease brain. Tau is a family of six isoforms, derived from a single gene by mRNA splicing. Tau protein is produced by a single gene expressed predominantly in neurons. They vary in size from 352-441 amino acides. In Alzheimer disease Tau is hyperphosphorylated, containing 3-4 fold more phosphoate/mole of the protein than the normal tau. Recent investigations show that MARK and PKA phosphorylate several sites within the repeats (notably the KXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates some sites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau's affinity for microtubules, and at the same time inhibits tau's assembly into PHFs (Paired helical filament).
Typical Data
Storage/Stability
Store at -20°C, if not intended for use within a month, keep it at 4°C and minimize freezing and thawing when use.
Expiration
12 months from the date of shipment when stored properly.
References
- Gong CX, Grundke-Iqbal I, Iqbal K(1994).Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A.Neuroscience. 61(4):765-72.
- 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.
