Beta-2-adrenergic receptor-CFP
(Plasmid
#55794)
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PurposeBeta-2-adrenergic receptor tagged with ECFP on carboxyl terminus
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Depositing Lab
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Sequence Information
Ordering
Item | Catalog # | Description | Quantity | Price (USD) | |
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Plasmid | 55794 | Standard format: Plasmid sent in bacteria as agar stab | 1 | $85 |
Backbone
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Vector backboneDerived from pECFP-N1
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Backbone manufacturerClontech
- Backbone size w/o insert (bp) 3954
- Total vector size (bp) 5967
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Vector typeMammalian Expression
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Selectable markersNeomycin (select with G418)
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)DH10B
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Copy numberHigh Copy
Gene/Insert
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Gene/Insert nameBeta-2-adrenergic receptor-ECFP
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Alt nameADRB2
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SpeciesH. sapiens (human); Aequorea victoria
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Insert Size (bp)2013
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Entrez GeneADRB2 (a.k.a. ADRB2R, ADRBR, ARB2, B2AR, BAR, BETA2AR)
- Promoter CMV
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Tag
/ Fusion Protein
- ECFP (C terminal on insert)
Cloning Information
- Cloning method Restriction Enzyme
- 5′ cloning site HindIII (not destroyed)
- 3′ cloning site NotI (not destroyed)
- 5′ sequencing primer CMV Forward (Common Sequencing Primers)
Resource Information
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A portion of this plasmid was derived from a plasmid made byBeta-2-adrenergic receptor-GFP was obtained from Gerda Breitweiser, Weis Center for Research, Geisinger Clinic, Danville, Pa. pECFP-N1 was purchased from Clontech.
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Article Citing this Plasmid
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.
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:
Beta-2-adrenergic receptor-CFP was a gift from Catherine Berlot (Addgene plasmid # 55794 ; http://n2t.net/addgene:55794 ; RRID:Addgene_55794) -
For your References section:
Live cell imaging of Gs and the beta2-adrenergic receptor demonstrates that both alphas and beta1gamma7 internalize upon stimulation and exhibit similar trafficking patterns that differ from that of the beta2-adrenergic receptor. Hynes TR, Mervine SM, Yost EA, Sabo JL, Berlot CH. J Biol Chem. 2004 Oct 15;279(42):44101-12. Epub 2004 Aug 5. 10.1074/jbc.M405151200 PubMed 15297467