Recombinant Mouse Emerin (Emd)

Code CSB-CF007633MO
MSDS
Size Pls inquire
Source in vitro E.coli expression system
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Product Details

Target Names
Emd
Uniprot No.
Alternative Names
Emd; Sta; Emerin
Species
Mus musculus (Mouse)
Expression Region
1-259
Target Protein Sequence
MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSY QFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQ PGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGL SYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFL LFVYYSIQAEEGNPFWMDP
Protein Length
Full length protein
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
Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C.
Gene References into Functions
  1. these data indicate that Emerin, a conserved nuclear lamina protein, couples extracellular matrix mechanics and SRF-Mkl1-dependent transcription. PMID: 28576971
  2. Emerin-null progenitors were delayed in their cell cycle exit, had decreased myosin heavy chain (MyHC) expression and formed fewer myotubes. Emerin binds to and activates histone deacetylase 3 (HDAC3). PMID: 28188262
  3. changes in nuclear size and shape, which are mediated by nuclear envelope structural proteins lamin A/C and/or emerin, also impact gene regulation and lineage differentiation in early embryos. PMID: 28088180
  4. Results suggest that emerin protein is an essential component of the cellular apparatus constraining and fine-tuning Wnt/b-catenin signaling in the heart providing tight control of cardiomyocyte numbers. PMID: 25274778
  5. emerin functions with myosin IIB to polarize actin flow and nuclear movement in fibroblasts, suggesting a novel function for the nuclear envelope in organizing directional actin flow and cytoplasmic polarity. PMID: 24152738
  6. Interactions between HDAC3 and Emerin mediate the interaction of myogenic regulatory loci with the nuclear lamina. PMID: 24062260
  7. a novel mechanism that could provide insight into the disease aetiology for the cardiac phenotype in many laminopathies, whereby lamin A/C and emerin regulate gene expression through modulation of nuclear and cytoskeletal actin polymerization PMID: 23644458
  8. report significant perturbations in the expression and activation of p38/Mapk14 in emerin-null myogenic progenitors, showing that perturbed expression of Wnt, IGF-1, TGF-beta, and Notch signaling components disrupts normal downstream myogenic signaling PMID: 22606356
  9. emerin facilitates repressive chromatin formation at the nuclear periphery by increasing the catalytic activity of HDAC PMID: 22570481
  10. These findings suggest roles for emerin as a downstream effector and signal integrator for tyrosine kinase signaling pathway(s) at the nuclear envelope. PMID: 19789182
  11. emerin and lamin A/C are bound to actin at the late stages of myotube differentiation PMID: 12670476
  12. the lamin a-emerin complex might have a role in muscular dystrophy and cardiomyopathy PMID: 12783988
  13. Data show that emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain. PMID: 16115958
  14. Emerin deficiency causes minimal motor and cardiac dysfunctions in mice with a structural fragility of myonuclei. PMID: 16507906
  15. Altered nuclear envelope elasticity caused by loss of emerin could contribute to increased nuclear fragility in Emery-Dreifuss muscular dystrophy patients with mutations in the emerin gene. PMID: 16997877
  16. Data show that both downregulation of LUMA and overexpression of dominant-negative acting LUMA fragments causes redistribution of emerin. PMID: 18230648
  17. Knockdown of A-type lamins and emerin in HeLa and C2C12 stimulated phosphorylation and nuclear translocation of ERK as well as activation of genes encoding downstream transcription factors. PMID: 19022376
  18. Deregulation of cell signaling contributes to nuclear envelope-linked disorders and suggests that mutations in NET25 and MAN1 may cause muscle diseases. PMID: 19720741

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Subcellular Location
Nucleus inner membrane; Single-pass membrane protein; Nucleoplasmic side. Nucleus outer membrane.
Tissue Specificity
Detected in embryonic fibroblasts, skeletal muscle, heart muscle and tongue epithelium (at protein level). Widely expressed.
Database Links
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