The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Rhesus IGF1R ORF mammalian expression plasmid, C-GFPSpark tag||CG90082-ACG|
|Rhesus IGF1R ORF mammalian expression plasmid, C-OFPSpark / RFP tag||CG90082-ACR|
|Rhesus IGF1R ORF mammalian expression plasmid, C-Flag tag||CG90082-CF|
|Rhesus IGF1R ORF mammalian expression plasmid, C-His tag||CG90082-CH|
|Rhesus IGF1R ORF mammalian expression plasmid, C-Myc tag||CG90082-CM|
|Rhesus IGF1R ORF mammalian expression plasmid, C-HA tag||CG90082-CY|
|Rhesus IGF1R ORF mammalian expression plasmid, N-Flag tag||CG90082-NF|
|Rhesus IGF1R ORF mammalian expression plasmid, N-His tag||CG90082-NH|
|Rhesus IGF1R ORF mammalian expression plasmid, N-Myc tag||CG90082-NM|
|Rhesus IGF1R ORF mammalian expression plasmid, N-HA tag||CG90082-NY|
|Rhesus IGF1R natural ORF mammalian expression plasmid||CG90082-UT|
|Learn more about expression Vectors|
The insulin-like growth factor-1 receptor (IGF1R) is a transmembrane tyrosine kinase involved in several biological processes including cell proliferation, differentiation, DNA repair, and cell survival. This a disulfide-linked heterotetrameric transmembrane protein consisting of two α and two β subunits, and among which, the α subunit is extracellular while the β subunit has an extracellular domain, a transmembrane domain and a cytoplasmic tyrosine kinase domain. IGF1R signalling pathway is activated in the mammalian nervous system from early developmental stages. Its major effect on developing neural cells is to promote their growth and survival. This pathway can integrate its action with signalling pathways of growth and morphogenetic factors that induce cell fate specification and selective expansion of specified neural cell subsets. Modulation of cell migration is another possible role that IGF1R activation may play in neurogenesis. In the mature brain, IGF-I binding sites have been found in different regions of the brain, and multiple reports confirmed a strong neuroprotective action of the IGF-IR against different pro-apoptotic insults. IGF1R is an important signaling molecule in cancer cells and plays an essential role in the establishment and maintenance of the transformed phenotype. Inhibition of IGF1R signaling thus appears to be a promising strategy to interfere with the growth and survival of cancer cells. IGF1R is frequently overexpressed by tumours, and mediates proliferation and apoptosis protection. IGF signalling also influences hypoxia signalling, protease secretion, tumour cell motility and adhesion, and thus can affect the propensity for invasion and metastasis. Therefore, the IGF1R is now an attractive anti-cancer treatment target.