EGFP-MYO10ΔF3
(Plasmid
#194857)
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PurposeExpress EGFP-MYO10 with the F3 FERM domain lobes deleted (1-1951) in mammalian cells.
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Depositing Lab
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Sequence Information
Ordering
Item | Catalog # | Description | Quantity | Price (USD) | |
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Plasmid | 194857 | Standard format: Plasmid sent in bacteria as agar stab | 1 | $85 |
Backbone
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Vector backboneEGFPC1
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Vector typeMammalian Expression
Growth in Bacteria
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Bacterial Resistance(s)Kanamycin, 50 μg/mL
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Growth Temperature37°C
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Growth Strain(s)DH5alpha
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Copy numberHigh Copy
Gene/Insert
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Gene/Insert nameMYO10 ΔF3
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Alt namemyosin X
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SpeciesH. sapiens (human)
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MutationTruncated MYO10 construct. MYO10 amino acids 1-1951 (amino acids 1952 - 2056 are deleted).
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Entrez GeneMYO10 (a.k.a. MyoX)
- Promoter CMV
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Tag
/ Fusion Protein
- EGFP (N terminal on insert)
Cloning Information
- Cloning method Unknown
- 5′ sequencing primer EGFPC (Common Sequencing Primers)
Resource Information
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A portion of this plasmid was derived from a plasmid made byThe original EGFPC1-hMyoX plasmid (Addgene plasmid # 47608) was created by Emanuel Strehler.
Terms and Licenses
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Academic/Nonprofit Terms
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Industry Terms
- Not Available to Industry
Trademarks:
- Zeocin® is an InvivoGen trademark.
Depositor Comments
The EGFP-MYO10ΔF3 construct was generated by replacing the wild-type MYO10-FERM domain (boundaries 1504-2056 in MYO10) with truncated MYO10 FERM domains where the F3 FERM lobe is deleted using a gene block (IDT). The gene blocks were inserted in EGFP-MYO10 (Addgene plasmid # 47608) using the PvuI and XbaI restriction sites. The final boundaries compared to full-length MYO10 are 1-1951.
These plasmids were created by your colleagues. Please acknowledge the Principal Investigator, cite the article in which the plasmids were described, and include Addgene in the Materials and Methods of your future publications.
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For your Materials & Methods section:
EGFP-MYO10ΔF3 was a gift from Guillaume Jacquemet (Addgene plasmid # 194857 ; http://n2t.net/addgene:194857 ; RRID:Addgene_194857) -
For your References section:
Myosin-X and talin modulate integrin activity at filopodia tips. Miihkinen M, Gronloh MLB, Popovic A, Vihinen H, Jokitalo E, Goult BT, Ivaska J, Jacquemet G. Cell Rep. 2021 Sep 14;36(11):109716. doi: 10.1016/j.celrep.2021.109716. 10.1016/j.celrep.2021.109716 PubMed 34525374