|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.
|Cynomolgus monkey IGFBP2 Gene cDNA Clone (full-length ORF Clone), expression ready, FLAG-tagged||CG90083-G-F|
|Cynomolgus monkey IGFBP2 Gene cDNA Clone (full-length ORF Clone), expression ready, His-tagged||CG90083-G-H|
|Cynomolgus monkey IGFBP2 Gene cDNA Clone (full-length ORF Clone), expression ready, Myc-tagged||CG90083-G-M|
|Cynomolgus monkey IGFBP2 Gene cDNA Clone (full-length ORF Clone), expression ready, untagged||CG90083-G-N|
|Cynomolgus monkey IGFBP2 Gene cDNA Clone (full-length ORF Clone), expression ready, HA-tagged||CG90083-G-Y|
IGFBP-2, also known as IGFBP2, is a insulin-like growth factor-binding protein (IGFBP). IGFBPs prolong the half-life of the IGFs , control bioavailability, activity, and distribution of insulin-like growth factor (IGF) through high-affinity IGFBP/IGF complexes. Six high-affinity IGF-binding proteins (IGFBP-1 to -6) have been identified. The six IGFBPs are structurally related but encoded by distinct genes. IGFBPs have a high affinity for IGFs. Some members of the IGFBP family have been consistently shown to inhibit IGF actions by preventing them from gaining access to the IGF receptors, while others potentiate IGF actions by facilitating the ligand-receptor interaction. IGFBP-2 is overexpressed in many malignancies and is often correlated with an increasingly malignant status of the tumor, pointing to a potential involvement of IGFBP-2 in tumorigenesis. It contains 1 IGFBP N-terminal domain and 1 thyroglobulin type-1 domain. It inhibits IGF-mediated growth and developmental rates.