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biological source
mouse
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2C8/D11, monoclonal
form
buffered aqueous solution
mol wt
~100 kDa
species reactivity
human, monkey
concentration
~1 mg/mL
technique(s)
flow cytometry: 10-20 μg/test using using human HeLa cells. immunoblotting: 1-2 μg/mL using whole extracts of human HeLa cells. immunofluorescence: 10-20 μg/mL using using human HeLa cells.
Monoclonal Anti-MASTL (mouse IgG2b isotype) is derived from the hybridoma 2C8/D11 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a fusion protein. Microtubule-Associated Serine/Threonine kinase-Like (MASTL), also known as GREATWALL (GWL) in Drosophila and Xenopus is localized to the nucleus but, during M-phase it is activated and re-localized to the centrosomes.
Immunogen
immunized with a fusion protein of 250aa polypeptide from the region that divides the kinase domain of mouse MASTL
Application
Monoclonal Anti-MASTL antibody produced in mouse may be used in various immunochemical techniques including immunoblotting, flow cytometry and immunofluorescence.
Biochem/physiol Actions
Microtubule-associated serine/Threonine kinase-Like (MASTL) acts as a cell cycle marker of M phase. It has an ability to regulate mitosis entry, anaphase and cytokinesis. In Drosophila MASTL (Greatwall) was initially identified as a kinase essential for chromosome condensation. MASTL enhances cyclin B1-Cdk1-dependent mitotic phosphorylation events. Furthermore, MASTL is also an inhibitor of the tumor suppressor protein Phosphatase 2A (PP2A), and thus maintains the equilibrium between cyclin B-Cdk1 and PP2A. A missense mutation in the MASTL gene leads to the development of autosomal dominant inherited thrombocytopenia.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Mitotic division is induced by protein phosphorylation. For a long time the supported hypothesis was that mitotic entry and exit were the exclusive result of cyclin B-Cdk1 kinase activation and inactivation, whereas the phosphatase activity required to dephosphorylate mitotic substrates
The basic biology of the cell division cycle and its control by protein kinases was originally studied through genetic and biochemical studies in yeast and other model organisms. The major regulatory mechanisms identified in this pioneer work are conserved in
Greatwall (Gwl) was originally discovered in Drosophila as an essential kinase for correct chromosome condensation and mitotic progression. In Xenopus, Gwl may influence the positive-feedback loop that directs cyclin B1-Cdk1 activation and the mitotic state by inhibiting the phosphatase PP
Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance
Burgess A, et al.
Proceedings of the National Academy of Sciences of the USA, 107(28), 12564-12569 (2010)
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