Anti-human phospho-202 TAU mAb 10F8

Anti-human phospho-202 TAU mAb 10F8

ID: INV4000035 Category:

Tau protein is a microtubule-associated protein mainly found in neurons, that regulates microtubule stability and axonal transport. It is classified as an intrinsically disordered protein, allowing it to adopt multiple conformations and interact with diverse cellular partners.

The antibody is produced exclusively from hybridoma and purified through one-step purification with Protein-A affinity chromatography.

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Tau protein is a microtubule-associated protein mainly found in neurons, that regulates microtubule stability and axonal transport. It is classified as an intrinsically disordered protein, allowing it to adopt multiple conformations and interact with diverse cellular partners. Tau proteins contain numerous potential phosphorylation sites that regulate it´s conformational changes and interactions. In pathological states, especially neurodegenerative disorders, hyperphosphorylation arises, leading to aggregation into neurofibrillary tangles - a hallmark of tauopathies like Alzheimer's disease.

The clone 10F8 is a Monoclonal Mouse antibody against Human Phospho-Tau (Ser202), Microtubule-associated protein tau (MAPT) (Uniprot: B3KTM0).

The antibody is produced exclusively from hybridoma and purified through one-step purification with Protein-A affinity chromatography.

Product-ID: INV4000035
Clone: 10F8
Immunogen: Animals were immunized with Synthetic peptide SGYSSPGS(Pi)PGTPG
Host: Mouse
Clonality: Monoclonal
Isotype: IgG1k
Formulation: Clear Liquid, PBS, pH 7.4
Concentration: > 1.0 mg/ml
Purity: > 95% by SDS-PAGE
Sizes available: 0.1 mg and 1.0 mg
Storage: at - 20 °C (repeated thawing and freezing should be avoided)
Tested application(s): ELISA, Western Blot, Immunhistochemistry

The product is for research use only and not for use in diagnostic or therapeutic procedures.

Additional information

Literature

[1] – Mark S. Forman, Virginia M.-Y. Lee, John Q. Trojanowski. New insights into genetic and molecular mechanisms of brain degeneration in tauopathies, Journal of Chemical Neuroanatomy, Volume 20, Issues 3–4, 2000, Pages 225-244, ISSN 0891-0618, https://doi.org/10.1016/S0891-0618(00)00100-9.
[2] – Alonso A, Zaidi T, Novak M, Grundke-Iqbal I, Iqbal K. Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments. Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6923-8. doi: 10.1073/pnas.121119298. Epub 2001 May 29. PMID: 11381127; PMCID: PMC34454.
[3] – Noble W, Hanger DP, Miller CC, Lovestone S. The importance of tau phosphorylation for neurodegenerative diseases. Front Neurol. 2013 Jul 1;4:83. doi: 10.3389/fneur.2013.00083. PMID: 23847585; PMCID: PMC3696910.

References:
a. Wolf J, Jäger C, Morawski M, Lachmann I, Schönknecht P, Mothes T, Arendt T. Tissue transglutaminase in Alzheimer’s disease – facts and fiction: a reply to “Tissue transglutaminase is a biochemical marker for Alzheimer’s disease”. Neurobiol Aging. 2014 Apr;35(4):e5-9. doi: 10.1016/j.neurobiolaging.2013.09.042. Epub 2013 Nov 7. PMID: 24300236.
b. Wolf J, Jäger C, Lachmann I, Schönknecht P, Morawski M, Arendt T, Mothes T. Tissue transglutaminase is not a biochemical marker for Alzheimer’s disease. Neurobiol Aging. 2013 Nov;34(11):2495-8. doi: 10.1016/j.neurobiolaging.2013.05.008. Epub 2013 Jun 5. PMID: 23747046.
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Product Information Sheet – INV4000035
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The product is for research use only and not for use in diagnostic or therapeutic procedures.

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