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Mouse Anti-MSN Recombinant Antibody (CBFYM-2656) (CBMAB-M2845-FY)

This product is mouse antibody that recognizes MSN. The antibody CBFYM-2656 can be used for immunoassay techniques such as: ELISA, IF, IHC, IP, WB.
See all MSN antibodies

Summary

Host Animal
Mouse
Specificity
Cattle, Human, Rat
Clone
CBFYM-2656
Antibody Isotype
IgG1, k
Application
ELISA, IF, IHC, IP, WB

Basic Information

Immunogen
Moesin from bovine uterus. Cellular Localization: Cell membrane and cytoplasmic
Specificity
Cattle, Human, Rat
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 7.4, 0.2% BSA
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
Moesin
Introduction
Moesin is a member of the ERM family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Moesin is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement.
Entrez Gene ID
Human4478
Rat81521
Cattle540426
UniProt ID
HumanP26038
RatO35763
CattleQ2HJ49
Alternative Names
Moesin; Membrane-Organizing Extension Spike Protein; Epididymis Luminal Protein 70; HEL70; IMD50
Function
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266).

Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266).

These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356).

The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160).

Modulates phagolysosomal biogenesis in macrophages (By similarity).

Participates also in immunologic synapse formation (PubMed:27405666).
Biological Process
Cellular response to testosterone stimulus Source: UniProtKB
Establishment of endothelial barrier Source: UniProtKB
Establishment of epithelial cell apical/basal polarity Source: UniProtKB
Gland morphogenesis Source: UniProtKB
Immunological synapse formation Source: UniProtKB
Leukocyte cell-cell adhesion Source: BHF-UCL
Leukocyte migration Source: BHF-UCL
Membrane to membrane docking Source: BHF-UCL
Positive regulation of cellular protein catabolic process Source: UniProtKB
Positive regulation of early endosome to late endosome transport Source: UniProtKB
Positive regulation of gene expression Source: UniProtKB
Positive regulation of podosome assembly Source: Ensembl
Positive regulation of protein localization to early endosome Source: UniProtKB
Regulation of cell shape Source: UniProtKB
Regulation of cell size Source: UniProtKB
Regulation of lymphocyte migration Source: UniProtKB
Regulation of organelle assembly Source: UniProtKB
T cell aggregation Source: UniProtKB
T cell migration Source: UniProtKB
T cell proliferation Source: UniProtKB
Cellular Location
Cytoskeleton
Plasma membrane
Cell membrane
Apical cell membrane
microvillus membrane
Other locations
microvillus
Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts.
Involvement in disease
Immunodeficiency 50 (IMD50):
A primary immunodeficiency disorder characterized by onset of recurrent bacterial or varicella zoster virus infections in early childhood, profound lymphopenia, hypogammaglobulinemia, fluctuating monocytopenia and neutropenia, and a poor immune response to vaccine antigens.
PTM
Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.
S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.

Li, M., Luo, S., Zhuo, Z., & Shu, M. (2024). Two cases of pediatric primary immunodeficiency caused by a familial moesin (MSN) gene mutation. Clinical Immunology, 258, 109858.

Huang, C. Y., Wei, P. L., Batzorig, U., Makondi, P. T., Lee, C. C., & Chang, Y. J. (2023). Identification of Moesin (MSN) as a Potential Therapeutic Target for Colorectal Cancer via the β-Catenin-RUNX2 Axis. International Journal of Molecular Sciences, 24(13), 10951.

Ahandoust, S., Li, K., Sun, X., Li, B. Y., Yokota, H., & Na, S. (2023). Intracellular and extracellular moesins differentially regulate Src activity and β-catenin translocation to the nucleus in breast cancer cells. Biochemical and Biophysical Research Communications, 639, 62-69.

Lee, C. H., Kim, D. S., Park, S. Y., & Ryu, H. S. (2023). Moesin-induced adriamycin resistance through IL-6/MSN/STAT3 axis and therapeutic efficacy of atovaquone in chemotherapy resistant triple-negative breast cancer. Cancer Research, 83(7_Supplement), 2774-2774.

Kovács, A. L., Kárteszi, J., Prohászka, Z., Kalmár, T., Késmárky, G., Koltai, K., ... & Gyulai, R. (2022). Hemizygous nonsense variant in the moesin gene (MSN) leads to a new autoimmune phenotype of Immunodeficiency 50. Frontiers in Immunology, 13, 919411.

Sun, X., Li, K., Hase, M., Zha, R., Feng, Y., Li, B. Y., & Yokota, H. (2022). Suppression of breast cancer-associated bone loss with osteoblast proteomes via Hsp90ab1/moesin-mediated inhibition of TGFβ/FN1/CD44 signaling. Theranostics, 12(2), 929.

Hu, X., Liu, Y., Bing, Z., Ye, Q., & Li, C. (2021). High Moesin expression is a predictor of poor prognosis of breast cancer: Evidence from a systematic review with meta-analysis. Frontiers in oncology, 11, 650488.

Chen, Y., Wang, J., Zhang, L., Zhu, J., Zeng, Y., & Huang, J. A. (2021). Moesin is a novel biomarker of endothelial injury in sepsis. Journal of Immunology Research, 2021.

Park, J. H., Lee, C., Han, D., Lee, J. S., Lee, K. M., Song, M. J., ... & Ryu, H. S. (2020). Moesin (MSN) as a novel proteome-based diagnostic marker for early detection of invasive bladder urothelial carcinoma in liquid-based cytology. Cancers, 12(4), 1018.

Okazaki, T., Saito, D., Inden, M., Kawaguchi, K., Wakimoto, S., Nakahari, T., & Asano, S. (2020). Moesin is involved in microglial activation accompanying morphological changes and reorganization of the actin cytoskeleton. The Journal of Physiological Sciences, 70(1), 1-11.

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

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