Recombinant Mouse Unconventional myosin-Ic (Myo1c), partial

Code CSB-YP893871MO
MSDS
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Source Yeast
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Code CSB-EP893871MO
MSDS
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Source E.coli
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Code CSB-EP893871MO-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-BP893871MO
MSDS
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Source Baculovirus
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Code CSB-MP893871MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Myo1c
Uniprot No.
Alternative Names
Myo1c; Unconventional myosin-Ic; Myosin I beta; MMI-beta; MMIb
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. Their highly divergent tails bind to membranous compartments, which then are moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.; Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation.
Gene References into Functions
  1. Myo1c ensembles can generate forces parallel to lipid bilayers. PMID: 27156719
  2. We propose a novel genome-wide mechanism where myosin synergizes with Pol II-associated actin to link the polymerase machinery with permissive chromatin for transcription activation. PMID: 26044184
  3. Our observations demonstrate specific changes in the expression of myosin IC isoform A that are concurrent with the occurrence of prostate cancer in the TRAMP mouse prostate cancer model that closely mimics clinical prostate cancer PMID: 25259793
  4. Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. PMID: 25437912
  5. The v-Crk-myosin-1c interaction, which modulates membrane dynamics by regulating Rac1 activity, is crucial for cell adhesion and spreading. PMID: 23983611
  6. Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus. PMID: 23593477
  7. Myo1c functions as a slow transporter rather than a tension-sensitive anchor. PMID: 22908250
  8. the novel specific NLS brings to the cell nucleus not only the "nuclear" isoform of myosin I (NM1 protein) but also its "cytoplasmic" isoform (Myo1c protein) PMID: 22295092
  9. The data suggest that Myosin 1c is involved in the cytoskeleton dynamics and membrane protein anchoring or sorting in B lymphocytes PMID: 21841128
  10. A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity PMID: 21265502
  11. The strength and attachment lifetime of single myo1c molecules as they bind beads coated with a bilayer of 2% phosphatidylinositol 4,5-bisphosphate and 98% phosphatidylcholine, were measured. PMID: 21156133
  12. Myo1c is a novel mediator of both insulin-stimulated and contraction-stimulated glucose uptake in skeletal muscle. PMID: 21127070
  13. Mutations in the Myo1c gene affect the interaction of Myo1c with nucleotides and actin. PMID: 20640478
  14. myosin Myo1c functions in a PI(3)K-independent insulin signalling pathway that controls the movement of intracellular GLUT4-containing vesicles to the plasma membrane PMID: 12490950
  15. localized membrane remodeling driven by the Myo1c motor appears to facilitate the fusion of exocytic GLUT4-containing vesicles with the adipocyte plasma membrane PMID: 15169906
  16. These data are consistent with Myo1c participating in the regulation of the Na+ channel after antidiuretic hormone stimulation. PMID: 15716323
  17. These results suggest that mechanical activity of myosin-1c is required for fast adaptation in vestibular hair cells. PMID: 16102537
  18. myo1c does not bind to physiological concentrations of phosphatidylserine but rather binds tightly to phosphatidylinositol 4,5-bisphosphate PMID: 16492791
  19. Motor protein Myo1c and its receptor protein NEMO act cooperatively to form the IKK-IRS-1 complex and function in TNF-alpha-induced insulin resistance. PMID: 16754954
  20. Subcellular localization of class I and class II myosin during B cell spreading showed differences, following CD44 cross-linking, myosin-1c was polarized to lamellipodia while the distribution of cytosplasmic nonmuscle class II myosin was not altered. PMID: 16919270
  21. Two distinct membrane binding sites within the regulatory and tail domains of myo1c protein were characterized. PMID: 16971510
  22. Calcium regulation of calmodulin binding to and dissociation from the myo1c regulatory domain was studied. PMID: 17910470
  23. These findings suggest that the Rictor-Myo1c complex is distinct from mTORC2 and that Myo1c, in conjunction with Rictor, participates in cortical actin remodeling events. PMID: 18426911
  24. insulin regulates Myo1c function via CaMKII-dependent phosphorylation, and these events play a role in insulin-regulated GLUT4 trafficking in adipocytes likely involving Myo1c motor activity. PMID: 19046570
  25. phosphoinositides are able to bind to and dissociate from myo1c(IQ-tail) as it remains bound to the membrane PMID: 19706607

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Subcellular Location
Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, stereocilium membrane. Cytoplasmic vesicle. Cell projection, ruffle.
Protein Families
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
Tissue Specificity
Isoform 3 is expressed in small intestine, pancreas, brain, kidney, skin, heart muscle, testis, striated muscle, spleen, liver and lung (at protein level). Expressed in brain, testis, adrenal glands, thymus, spleen, kidney, lung, heart, cochlea and vestib
Database Links
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