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Mouse Anti-MASTL Recombinant Antibody (CBFYM-0094) (CBMAB-M0105-FY)

This product is mouse antibody that recognizes MASTL. The antibody CBFYM-0094 can be used for immunoassay techniques such as: ELISA, ICC, IF, WB.
See all MASTL antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-0094
Antibody Isotype
IgG1, k
Application
ELISA, ICC, IF, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1, k
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.2
Preservative
0.09% Sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Microtubule Associated Serine/Threonine Kinase Like
Introduction
This gene encodes a microtubule-associated serine/threonine kinase. Mutations at this locus have been associated with autosomal dominant thrombocytopenia, also known as thrombocytopenia-2. Alternatively spliced transcript variants have been described for this locus.
Entrez Gene ID
84930
UniProt ID
Q96GX5
Alternative Names
Microtubule Associated Serine/Threonine Kinase Like; Greatwall Kinase Homolog; MAST-L; THC2; GWL; GW; Microtubule-Associated Serine/Threonine-Protein Kinase-Like
Function
Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation.
Biological Process
Cell division Source: UniProtKB-KW
Cellular response to DNA damage stimulus Source: UniProtKB
Female meiosis II Source: Ensembl
G2/M transition of mitotic cell cycle Source: UniProtKB
Intracellular signal transduction Source: GO_Central
Mitotic cell cycle Source: UniProtKB
Negative regulation of phosphoprotein phosphatase activity Source: UniProtKB
Peptidyl-serine phosphorylation Source: GO_Central
Positive regulation of ubiquitin protein ligase activity Source: Ensembl
Regulation of cell cycle Source: UniProtKB
Cellular Location
Cytoskeleton
centrosome
Nucleus
Other locations
Cleavage furrow
Note: During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. Upon mitotic exit moves to the cleavage furrow.
Involvement in disease
Defects in MASTL may play a role in the pathogenesis of thrombocytopenia, a disorder defined by reduced number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting.
PTM
Phosphorylation at Thr-741 by CDK1 during M phase activates its kinase activity (By similarity). Maximum phosphorylation occurs in prometaphase.

Sanz‐Castillo, B., Hurtado, B., Vara‐Ciruelos, D., El Bakkali, A., Hermida, D., Salvador‐Barbero, B., ... & Malumbres, M. (2023). The MASTL/PP2A cell cycle kinase‐phosphatase module restrains PI3K‐Akt activity in an mTORC1‐dependent manner. The EMBO Journal, 42(2), e110833.

Erguven, M., Kilic, S., Karaca, E., & Diril, M. K. (2023). Genetic complementation screening and molecular docking give new insight on phosphorylation-dependent Mastl kinase activation. Journal of Biomolecular Structure and Dynamics, 41(17), 8241-8253.

Gouttia, O. G., Zhao, J., Li, Y., Zwiener, M. J., Wang, L., Oakley, G. G., & Peng, A. (2022). The MASTL-ENSA-PP2A/B55 axis modulates cisplatin resistance in oral squamous cell carcinoma. Frontiers in Cell and Developmental Biology, 10, 904719.

Kang, M., Kim, C., Leem, J., Kim, Y. H., Kwon, Y. J., Yoon, Y. N., ... & Kim, J. S. (2021). Discovery and characterization of a novel MASTL inhibitor MKI-2 targeting MASTL-PP2A in breast cancer cells and oocytes. Pharmaceuticals, 14(7), 647.

Fatima, I., Barman, S., Uppada, J., Chauhan, S., Rauth, S., Rachagani, S., ... & Dhawan, P. (2021). MASTL regulates EGFR signaling to impact pancreatic cancer progression. Oncogene, 40(38), 5691-5704.

Taskinen, M. E., Närvä, E., Conway, J. R., Hinojosa, L. S., Lilla, S., Mai, A., ... & Ivaska, J. (2020). MASTL promotes cell contractility and motility through kinase-independent signaling. Journal of Cell Biology, 219(6), e201906204.

Fatima, I., Singh, A. B., & Dhawan, P. (2020). MASTL: A novel therapeutic target for Cancer Malignancy. Cancer Medicine, 9(17), 6322-6329.

Conway, J. R. W., Närvä, E., Taskinen, M. E., & Ivaska, J. (2020). Kinase-independent functions of MASTL in cancer: a new perspective on MASTL targeting. Cells, 9(7), 1624.

Hermida, D., Mortuza, G. B., Pedersen, A. K., Pozdnyakova, I., Nguyen, T. T., Maroto, M., ... & Montoya, G. (2020). Molecular basis of the mechanisms controlling MASTL. Molecular & Cellular Proteomics, 19(2), 326-343.

Cetti, E., Di Marco, T., Mauro, G., Mazzoni, M., Lecis, D., Minna, E., ... & Greco, A. (2019). Mitosis perturbation by MASTL depletion impairs the viability of thyroid tumor cells. Cancer Letters, 442, 362-372.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

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