Recombinant Mouse Unconventionnal myosin-X (Myo10), partial

Code CSB-YP522290MO
MSDS
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Source Yeast
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Code CSB-EP522290MO
MSDS
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Source E.coli
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Code CSB-EP522290MO-B
MSDS
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Source E.coli
Conjugate 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.
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Code CSB-BP522290MO
MSDS
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Source Baculovirus
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Code CSB-MP522290MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Myo10
Uniprot No.
Alternative Names
Myo10; Unconventional myosin-X; Unconventional myosin-10
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
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.
Form
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.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
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.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
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.
Lead Time
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.
Notes
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.

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Target Background

Function
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts.; Functions as a dominant-negative regulator of isoform 1, suppressing its filopodia-inducing and axon outgrowth-promoting activities. In hippocampal neurons, it increases VASP retention in spine heads to induce spine formation and spine head expansion.
Gene References into Functions
  1. These results suggest that the lever-arm of full-length myosin-X is flexible enough to processively steps on different actin filaments within the actin bundles of filopodia. This characteristic of myosin-X may facilitate actin filament convergence for filopodia production. PMID: 28287133
  2. Reduction in ADD1 protein in NEK1 mutant mice is associated with hyperphosphorylation of ADD1, thereby preventing the interaction with MYO10 during meiotic spindle formation PMID: 28982183
  3. analysis of phenotypes of Cdc42 and Myo10 deletion that show multiple roles of filopodial dynamics PMID: 28289096
  4. Myo10 is required for neurogenic cell migration through N-cadherin mediated cell adhesion. PMID: 25491426
  5. Myo10 is involved in neuronal development both in vitro and in vivo by regulating microtubule stability PMID: 26178610
  6. Results indicate that, in neuronal cells, TNTs can arise from a subset of Myo10-driven dorsal filopodia, independent of its binding to integrins and N-cadherins. PMID: 23886947
  7. The study analyzed and cloned 2-kb of the 5'-upstream sequences of mouse full-length Myo10 (fMyo10) and headless Myo10 (hMyo10) to understand the transcriptional regulation of the Myo10 gene. PMID: 23742061
  8. headless Myo10 can function as a negative regulator of full-length Myo10 and that the two isoforms of Myo10 have opposing roles in axon outgrowth. PMID: 22661706
  9. Myo10 was required for neuronal morphological transition during radial neuronal migration in the developmental neocortex PMID: 22590642
  10. DCC promotes movement of Myo X along basal actin filaments and enhances Myo-X-mediated basal filopodium elongation. PMID: 22349703
  11. Myo10 plays a role in osteoclast attachment and podosome positioning by direct linkage of actin to the microtubule network PMID: 20081229
  12. Myo10 provides a molecular link between PI(3)K and pseudopod extension during phagocytosis PMID: 12055636
  13. Myosin-X is involved in cell-cell adhesion-associated signaling-linked membrane and/or cytoskeleton reorganization. PMID: 12752505
  14. myosin X PH domains have roles in signaling events and in regulating its cellular function PMID: 14729907
  15. Knock-down of Myo10 by siRNA impaired integrin function in cell adhesion, whereas overexpression of Myo10 stimulated the formation and elongation of filopodia in an integrin-dependent manner. PMID: 15156152
  16. Results report that, in addition to full-length myosin 10 (Myo10), brain expresses a shorter form of Myo10 that lacks a myosin head domain. PMID: 16371656
  17. Here, we provide evidence for the involvement of the unconventional myosin X (Myo X) in netrin-1 function. We find that Myo X interacts with the netrin receptor deleted in colorectal cancer (DCC) and neogenin, a DCC-related protein. PMID: 17237772
  18. The motor function of the two-headed form of myoX is critical for actin reorganization at the leading edge, leading to filopodia formation. PMID: 17954606
  19. Our data indicate that Myo10 is required to guide endothelial migration toward BMP6 gradients via the regulation of filopodial function and amplification of BMP signals. PMID: 18158328
  20. Data show that myosin X suppresses adhesion pf GnRH cells to the matrix and decreases their migratory activity. PMID: 19254772

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Subcellular Location
Cytoplasm, cytosol. Cell projection, lamellipodium. Cell projection, ruffle. Cytoplasm, cytoskeleton. Cell projection, filopodium tip. Cytoplasm, cell cortex. Cell projection, filopodium membrane; Peripheral membrane protein.
Protein Families
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
Tissue Specificity
Detected in brain, heart, kidney, liver, stomach, skeletal muscle, lung, testis and skin. Isoform Headless is expressed in embryonic and neuronal stem cells, and enriched in proliferating and migrating cells.
Database Links
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