IL 11 Human, Pichia
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
Greater than 95% as determined by SDS-PAGE.
Description
IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.
The IL11 is purified by proprietary chromatographic techniques.
Product Specs
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.
Product Science Overview
The recombinant human IL-11 (rhIL-11) is often produced using the yeast species Pichia pastoris. This method involves the synthesis of full-length cDNA of human IL-11, which is then inserted into an expression plasmid. The plasmid is linearized and transformed into Pichia pastoris, where the recombinant gene is highly expressed . The expression product is subsequently purified using a three-step chromatography method, ensuring that the biological activity of the protein is maintained .
IL-11 is known to stimulate the T-cell-dependent development of immunoglobulin-producing B cells . It also interacts with the extracellular domain of the human IL-11 receptor subunit α and activates STAT3 signaling in cells co-expressing human IL-11 receptors . This signaling pathway is crucial for various cellular processes, including cell survival, proliferation, and differentiation.
Recombinant IL-11 has been explored for its therapeutic potential in treating conditions such as thrombocytopenia, a condition characterized by low platelet counts. The macaque orthologue of IL-11 has been found to be an 8-fold more effective STAT3 activator compared to human IL-11, making it a potent substitute for human IL-11 in therapeutic applications . Additionally, IL-11’s role in immune response and inflammation makes it a target for developing drugs aimed at treating oncologic, hematologic, and inflammatory diseases .
Using Pichia pastoris for the expression of recombinant proteins offers several advantages:
- High Expression Levels: Pichia pastoris can achieve high levels of protein expression, making it suitable for large-scale production.
- Post-Translational Modifications: Unlike bacterial systems, Pichia pastoris can perform post-translational modifications, which are essential for the biological activity of many proteins.
- Cost-Effective: The yeast system is relatively cost-effective compared to mammalian cell cultures, making it an attractive option for producing recombinant proteins.
In summary, the production of recombinant human IL-11 using Pichia pastoris is a well-established method that ensures high yield and biological activity of the protein. This recombinant cytokine holds significant therapeutic potential for various medical conditions, highlighting its importance in biomedical research and drug development.
