Recombinant human LR3 long chain insulin-like growth factor 1(rh-LR3-IGF-1) was first cloned and expressed by Francis et al. in 1992. The protein changed the third amino acid of the hIGF-1 amino acid sequence to arginine (Arg) and added 13 amino acids (mainly composed of the N-terminal of porcine growth hormone) to the N-terminal. The modified protein was tested to have 10 times higher activity than the natural hIGF-1, in vivo half-life extended to 6-10h. The recombinant human LR3 long chain insulin-like growth factor 1 was expressed by E. coli and purified by multiple steps. Compared with natural hIGF-1, it has higher activity and stability, and is more suitable for serum-free medium, cell culture and other research.

Size:10 µg, 100 µg, 1 mg, 10mg, 100mg
Formulation: Lyophilized powder
Mol. Wt.: 9.12 kDa
Theory pI: 8.62
Resources: Escherichia coli (E. coli)
Species：human
Purity: ≥ 95%(SDS-PAGE detection)
Endotoxin: <50 EU/mg
Activity: EC50:< 100 ng/ml
Absorption coefficient: UV absorption method, extinction coefficient E(0.1% at 280nm)= 0.531
Storage Condition: -20oC
Transport: Ambient Temp
Storage Duration: 3 years