|Datasheet||Specific References||Reviews||Related Products||Protocols|
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.
|Human GNGT1 Gene cDNA Clone (full-length ORF Clone), expression ready, FLAG-tagged||HG13658-G-F|
|Human GNGT1 Gene cDNA Clone (full-length ORF Clone), expression ready, His-tagged||HG13658-G-H|
|Human GNGT1 Gene cDNA Clone (full-length ORF Clone), expression ready, Myc-tagged||HG13658-G-M|
|Human GNGT1 Gene cDNA Clone (full-length ORF Clone), expression ready, untagged||HG13658-G-N|
|Human GNGT1 Gene cDNA Clone (full-length ORF Clone), expression ready, HA-tagged||HG13658-G-Y|
GNGT1 is a subunit of of transducin. Heterotrimeric G proteins consist of alpha, beta, and gamma subunits. They are membrane bound GTPases that are linked to 7-TM receptors. They function as signal transducers for the 7-transmembrane-helix G protein-coupled receptors. They are involved as a modulator or transducer in various transmembrane signaling systems. G proteins are bound to GDP in the 'off' state. GNGT1 is the gamma subunit of transducin. Ligand-receptor binding results in detachment of the G protein, switching it to an 'on' state and permitting Galpha activation of second messenger signalling cascades. There are several types of Galpha proteins; in addition, some Gbetagamma subunits have active functions. Gbetagamma coupled to H1 receptors can activate PLA2 and Gbetagamma coupled to M1 receptors can activate KIR channels. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.