Monoclonal Anti-τ (Tau) antibody produced in mouse

Monoclonal Anti- τ (TAU) (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. τ (TAU) proteins are a part of microtubule associated proteins (MAPs). They are densely found in neurons and in trace amounts in non-neuronal cells. In brain six isoforms of τ (TAU) proteins are present.

The antibody reacts exclusively with the chemically heterogeneous τ in both the phosphorylated and non-phosphorylated form. The antibody does not react with other MAPs or with tubulin. In immunohistochemical staining, it localizes τ along microtubules in axons, somata, dendrites and astrocytes, and on ribosomes. The antibody may be used for staining of τ in Alzheimer neurofibrillary tangles in sections of human brain tissue.

The best known microtubule associated proteins (MAPs) which copurify with microtubules are MAP2 and Tau. These two proteins are heat stable and stimulate formation of the microtubule polymer from purified tubulin subunits. Tau is chemically heterogenous, however, limited protolysis has demonstrated that the different eletrophoretic species are closely related. Tau is immunologically distinct from the other MAPs, namely MAP1, MAP2 and MAP5. Localization studies have demonstrated that Tau is intimately associated with the filamentous structures which compose the neurofibrillary tangles as found in an Alzheimer′s disease brain.

bovine microtubule-associated proteins (MAPs)

Monoclonal Anti-τ (Tau) antibody has been used:

• in immunohistology
• in immunoblotting
• in dot blot
• in immunohistochemistry

Mouse monoclonal clone TAU-2 anti-Tau antibody maybe used to study microtubule associated proteins (MAP) expression and cytological localization in various tissue and cell lines, under different developmental and environmental circumstances.

Monoclonal Anti- τ (TAU) is phosphatase independent; it will bind Tau proteins in either their phosphorylated or non-phosphorylated forms. It localizes Tau proteins along microtubules in axons, somata, dendrites, astrocytes and on ribosomes (polysomes). The best-known microtubule associated proteins (MAPs) which copurify with microtubules are MAP2 and Tau. These two proteins are heat stable and stimulate formation of the microtubule polymer from purified tubulin subunits. Tau is immunologically distinct from the other MAPs. Tau is intimately associated with the filamentous structures which compose the neurofibrillary tangles as found in an Alzheimer′s disease brain.

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