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  4. Recombinant Mouse Moesin (Msn)

Recombinant Mouse Moesin (Msn)

  • 中文名称：
    小鼠Msn重组蛋白
  • 货号：
    CSB-YP015048MO
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 中文名称：
    小鼠Msn重组蛋白
  • 货号：
    CSB-EP015048MO
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 中文名称：
    小鼠Msn重组蛋白
  • 货号：
    CSB-EP015048MO-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 中文名称：
    小鼠Msn重组蛋白
  • 货号：
    CSB-BP015048MO
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 中文名称：
    小鼠Msn重组蛋白
  • 货号：
    CSB-MP015048MO
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
  • Uniprot No.：
  • 别名：
    Msn; Moesin; Membrane-organizing extension spike protein
  • 种属：
    Mus musculus (Mouse)
  • 蛋白长度：
    Full Length of Mature Protein
  • 表达区域：
    2-577
  • 氨基酸序列
    PKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE MAELTARISQ LEMARKKKES EAVEWQQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTA NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    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. Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement. These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction. 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. Modulates phagolysosomal biogenesis in macrophages. Participates also in immunologic synapse formation.
  • 基因功能参考文献：
    1. Collectively, these results implicate both moesin and myosin IIA in the regulation of phagolysosome biogenesis and in host defense against infections. PMID: 29247647
    2. these findings underscore the importance of moesin in IL-15-dependent CD8+ Treg cell homeostasis and the control of self-tolerance PMID: 28978692
    3. Moesin is an important regulator of the surface abundance and stability of TbetaRII and is important in facilitating the efficient generation of iTregs. PMID: 28287407
    4. The expression of moesin was upregulated in cardiomyocytes under inflammation, inducing protrusion formation in a phosphorylation-dependent fashion. PMID: 27342875
    5. These results of this study may pave the way for exploiting moesin as a novel target for intervention in muscular dystrophy. PMID: 28082118
    6. this study shows that low neutrophil rolling in inflamed venules was impaired in moesin-deficient mice PMID: 27131737
    7. High blood moesin levels were also observed in cecal ligation and puncture (CLP)-induced sepsis in mice. Administration of blocking moesin antibodies attenuated CLP-induced septic death. PMID: 25947626
    8. An increase in moesin expression may contribute to the increased expression of P-gp in blood brain barrier endothelial cells, leading to the development of morphine analgesic tolerance. PMID: 25048710
    9. phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein moesin PMID: 25792740
    10. both moesin-mediated inhibition and its localized deactivation by myosin phosphatase are essential for neutrophil polarization and effective neutrophil tracking of pathogens. PMID: 25601651
    11. A novel role for moesin in regulating clathrin-dependent S1PR1 internalization through clathrin-coated vesicles formation. PMID: 24358210
    12. Moesin may be a potential drug target for inhibiting corneal fibrosis, and the details of moesin-related signaling pathways would be critical for understanding corneal fibrosis. PMID: 23583046
    13. Findings indicate a function of moesin in lymphocyte homeostasis in regulating lymphocyte egress from lymphoid organs. PMID: 22875842
    14. A Pak1-PP2A-ERM signaling axis mediates F-actin rearrangement and degranulation in mast cells. PMID: 23063725
    15. the extracellular matrix molecule VN and its neuronal receptor TLCN play a pivotal role in the phosphorylation of ezrin/radixin/moesin proteins and the formation of phagocytic cup-like structures on neuronal dendrites PMID: 23019340
    16. Ezrin/radixin/moesin are required for the purinergic P2X7 receptor (P2X7R)-dependent processing of the amyloid precursor protein. PMID: 22891241
    17. increased moesin expression promotes EMT by regulating adhesion and contractile elements for changes in actin filament organization. PMID: 22031288
    18. biomarker for the assessment of genotoxic carcinogens in lymphoma PMID: 22358511
    19. Moesin is involved in AGE-induced retinal vascular endothelial dysfunction and the phosphorylation of moesin is triggered via ROCK and p38 MAPK activation. PMID: 21327982
    20. The ERM (ezrin, radixin, moesin) proteins are novel scaffolds at the level of SOS activity control, which is relevant for both normal Ras function and dysfunction known to occur in several human cancers. PMID: 22132106
    21. ezrin-radixin-moesin (ERM) proteins are induced in activated microglia/macrophages, whereas ERM molecules are only marginally expressed in quiescent microglia in the normal brain. PMID: 21451358
    22. Ezrin, radixin, and moesin are phosphorylated in response to 2-methoxyestradiol and modulate endothelial hyperpermeability. PMID: 21659656
    23. Results show that while CD43 binding to ezrin-radixin-moesin proteins is crucial for S76 phosphorylation, CD43 movement and regulation of T-cell migration can occur through an ERM-independent, phosphorylation-dependent mechanism. PMID: 21289089
    24. Data suggest that myosin-II and ERM proteins modulate mechanical properties in oocytes, contributing to cell polarity and to completion of meiosis. PMID: 20660156
    25. Data show that TNF-alpha induces the formation of fibrotic foci by cultured retinal pigment epithelial cells through activation of transforming growth factor-TGF-beta signaling in a manner dependent on hyaluronan-CD44-moesin interaction. PMID: 19965872
    26. cross talk between the blastocyst and uterus involving the ezrin/radixin/moesin (ERM) proteins and ERM-associated cytoskeletal cross-linker proteins CD43, CD44, ICAM-1, and ICAM-2. PMID: 14613898
    27. The study demonstrates a link between Galpha13 signaling that regulates differentiation of F9 cells through primitive to parietal endoderm and a moesin requirement for cell survival. PMID: 16860319
    28. Ezrin/radixin/moesin proteins are activated by osmotic shrinkage in a PtdIns(4,5)-P(2)-dependent manner. PMID: 17977945
    29. These data identify the ERM proteins, which cross-link the plasma membrane and actin, as major and stable cytoskeletal-associated proteins in lens fibers, and indicate a potential role(s) for the ERMs in fiber cell actin cytoskeletal organization. PMID: 18261459
    30. Hepatic stellate cell migration and fibrogenesis in moesin-deficient mice, is described. PMID: 18606220
    31. This is the first report of a functional involvement of moesin in the regulation of lung inflammation and repair, which regulates the preservation of alveolar structure and lung homeostasis. PMID: 18658275
    32. These studies identify a new ERM kinase of importance in lymphocytes and confirm the role of ezrin-radixin-moesin phosphorylation in regulating cell shape and motility. PMID: 19255442
    33. argue for ezrin-radixin-moesin proteins being both targets and modulators of parvovirus infection PMID: 19321616
    34. These results suggest a critical role of moesin phosphorylation in Advanced glycation end products-induced endothelial cell functional and morphological regulations PMID: 19395553

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  • 亚细胞定位：
    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, microvillus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, microvillus.
  • 数据库链接：

    KEGG: mmu:17698

    STRING: 10090.ENSMUSP00000113071

    UniGene: Mm.138876