癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Moesin Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone MSN/493 ]
- 产品详情
- 实验流程
- 背景知识
Application 
| WB, IHC, IF, FC |
|---|---|
| Primary Accession | P26038 |
| Other Accession | 4478, 87752 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | Mouse / IgG1, kappa |
| Clone Names | MSN/493 |
| Calculated MW | 67820 Da |
| Gene ID | 4478 |
|---|---|
| Other Names | Moesin, Membrane-organizing extension spike protein, MSN |
| Application Note | WB~~1:1000 IHC~~1:100~500 IF~~1:50~200 FC~~1:10~50 |
| Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
| Precautions | Moesin Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MSN (HGNC:7373) |
|---|---|
| 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). Also participates in immunologic synapse formation (PubMed:27405666). |
| Cellular Location | Cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P26041}. Apical cell membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus {ECO:0000250|UniProtKB:P26041}. 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. {ECO:0000250|UniProtKB:P26041, ECO:0000269|PubMed:18586956, ECO:0000269|PubMed:9298994} |
| Tissue Location | In all tissues and cultured cells studied. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Recognizes 78kDa moesin protein. Moesin, a member of the talin-4.1 superfamily, is a linking protein of the sub-membranous actin cytoskeleton. It is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines but not in blood cells. The ERM proteins, ezrin, radixin, and moesin are involved in a variety of cellular functions, such as cell adhesion, migration, and the organization of cell surface structures, and are highly homologous, both in protein sequence and in functional activity, with merlin/schwannomin, a neurofibromatosis-2-associated tumor-suppressor protein. Cell lines of epithelial and mesothelial origin contain both moesin and radixin whereas cells of endothelial and lymphoid origin express moesin.
REFERENCES
Schwartz-Albiez R et. al., European Journal Cell Biology, 1995; 67:189-198. | Lankes W et. al., Biochem Journal, 1988; 251:831-842. |
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