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| Catalog | Product Name | EC No. | CAS No. | Source | Price |
|---|---|---|---|---|---|
| NATE-1020 | Recombinant Ribosomal-protein-serine acetyltransferase from E. coli | E. coli | Inquiry |
Ribosome inactivating proteins (RIPs) are a group of proteins that have the ability to inhibit protein synthesis by removing specific adenine residues from the highly conserved α-sarcin/ricin loop (SRL) of the large rRNA. One class of RIPs is the ribosome inactivating proteins type II (RIP-II), which consists of an RNA N-glycosidase enzyme known as ribosome-inactivating protein from bitter gourd seeds (RimL). RimL is a 28 kDa protein that has been isolated from the seeds of bitter gourd (Momordica charantia) and has been found to possess strong cytotoxic and antitumor activities.
RimL belongs to the family of ribosome-inactivating proteins, which are widely distributed in nature and have been shown to display a wide range of biological activities, including anti-viral, anti-fungal, and anti-tumor properties. RimL is a type II RIP, meaning that it possesses both RNA N-glycosidase activity and N-glycosidase activity towards glycosylated proteins. RimL is a single-chain protein composed of a single polypeptide chain with a molecular weight of approximately 28 kDa. The amino acid sequence of RimL is highly homologous to other RIPs, such as ricin, saporin, and abrin, and contains a conserved catalytic domain that is responsible for its cytotoxic activity.
RimL functions as an RNA N-glycosidase enzyme, which cleaves specific adenine residues from the SRL of the large rRNA in the ribosome, leading to the inhibition of protein synthesis. This mechanism of action results in the selective inhibition of cancer cells, as they are more sensitive to the loss of protein synthesis compared to normal cells. In addition to its RNA N-glycosidase activity, RimL also possesses N-glycosidase activity towards glycosylated proteins, leading to the inactivation of protein synthesis in cancer cells.
The mechanism of action of RimL involves the binding of the protein to the ribosome, where it recognizes and cleaves specific adenine residues from the SRL of the large rRNA. This cleavage leads to the inactivation of the ribosome and prevents the binding of elongation factors, resulting in the inhibition of protein synthesis. RimL is also able to catalyze the removal of N-glycosidase from glycosylated proteins, leading to their inactivation. This dual mechanism of action makes RimL a potent cytotoxic agent against cancer cells.
RimL has been investigated for its potential applications in cancer therapy due to its strong cytotoxic and anti-tumor activities. Studies have shown that RimL is able to selectively inhibit the growth of cancer cells in vitro and in vivo, while sparing normal cells. This selectivity makes RimL a promising candidate for the development of targeted cancer therapies. In addition to its anti-cancer activities, RimL has also been shown to possess anti-viral and anti-fungal properties, making it a versatile molecule with a wide range of potential applications.
The clinical significance of RimL lies in its potential as a novel anti-cancer therapy. Studies have shown that RimL is able to inhibit the growth of a variety of cancer cells, including breast, lung, prostate, and colon cancer cells, both in vitro and in animal models. RimL has also been shown to possess synergistic effects with other chemotherapeutic agents, further enhancing its anti-tumor activities. Clinical trials are currently underway to investigate the safety and efficacy of RimL as a cancer therapy, with promising results thus far.
RimL is a ribosome-inactivating protein with potent cytotoxic and anti-tumor activities. Its mechanism of action involves the cleavage of specific adenine residues from the SRL of the large rRNA in the ribosome, leading to the inhibition of protein synthesis in cancer cells. RimL also possesses N-glycosidase activity towards glycosylated proteins, further enhancing its cytotoxic effects. The potential applications of RimL in cancer therapy are vast, with promising results from preclinical studies and ongoing clinical trials. RimL represents a promising candidate for the development of targeted cancer therapies and holds great potential for the treatment of various types of cancer in the future.
