pcDNA3 c-SRC (151-536)
Full plasmid sequence is not available for this item.
|Item||Catalog #||Description||Quantity||Price (USD)|
|Plasmid||42207||Standard format: Plasmid sent in bacteria as agar stab||1||$85|
This material is available to academics and nonprofits only.
- Backbone size w/o insert (bp) 5446
- Total vector size (bp) 7000
Vector typeMammalian Expression
Selectable markersNeomycin (select with G418)
Growth in Bacteria
Bacterial Resistance(s)Ampicillin, 100 μg/mL
Copy numberHigh Copy
Gene/Insert namec-SRC (151-536)
Alt namesarcoma (Schmidt-Ruppin A-2) viral oncogene homolog
SpeciesH. sapiens (human)
Mutationcontains amino acids 151-536
GenBank IDNM_005417.3 AAA60584.1
Entrez GeneSRC (a.k.a. ASV, SRC1, THC6, c-SRC, p60-Src)
- Promoter CMV
- Cloning method Restriction Enzyme
- 5′ cloning site HindIII (not destroyed)
- 3′ cloning site XhoI (not destroyed)
- 5′ sequencing primer CMV-F
- 3′ sequencing primer BGH-rev (Common Sequencing Primers)
Article Citing this Plasmid
Terms and Licenses
- Not Available to Industry
- Zeocin® is an InvivoGen trademark.
All c-SRC mutants were generated by polymerase chain reaction using c-SRC (WT) (Addgene Plasmid #42202) as a template, and polymerase chain reaction products containing a minimal Kozak sequence were cloned into the HindIII and XhoI sites of pcDNA3. This construct contains amino acids 151-536 of human c-SRC and is untagged. All sequences were confirmed using an automated ABI DNA sequencer (Howard Hughes Nucleic Acid Facility, Duke University).
This plasmid also contains an L176F point mutation which should not affect function.
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.
For your Materials & Methods section:pcDNA3 c-SRC (151-536) was a gift from Robert Lefkowitz (Addgene plasmid # 42207 ; http://n2t.net/addgene:42207 ; RRID:Addgene_42207)
For your References section:beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis. Miller WE, Maudsley S, Ahn S, Khan KD, Luttrell LM, Lefkowitz RJ. J Biol Chem. 2000 Apr 14;275(15):11312-9. 10.1074/jbc.275.15.11312 PubMed 10753943
Map uploaded by the depositor.