Cyclin-I is composed of 377 amino acids and has a molecular weight of approximately 41.4 kDa . It is expressed consistently during cell cycle progression, unlike other cyclins that exhibit distinct expression and degradation patterns . This consistent expression suggests that Cyclin-I may have unique regulatory roles compared to other cyclins.
Recombinant Cyclin-I is typically produced using Escherichia coli (E. coli) as the expression host . The recombinant protein is often tagged with histidine (His) at both the N-terminal and C-terminal ends to facilitate purification. The protein is usually lyophilized from a sterile PBS solution with added protectants like trehalose, mannitol, and Tween80 .
Recombinant Cyclin-I is used primarily for research purposes. It is valuable in studying cell cycle regulation, protein interactions, and the role of cyclins in various cellular processes. The protein can be used in various assays, including Western blotting, ELISA, and immunoaffinity purification .
Lyophilized recombinant Cyclin-I is stable for up to 12 months when stored at -20°C to -80°C. Once reconstituted, the protein solution can be stored at 4-8°C for 2-7 days or at -20°C for up to 3 months .
Cyclin-I’s consistent expression and unique regulatory roles make it a significant protein for understanding cell cycle dynamics and developing potential therapeutic interventions.