Greater than 85.0% as determined by SDS-PAGE.
Interleukin-12 (IL-12) is a cytokine that plays a crucial role in the immune system's response to infections and cancer. It acts as a signaling molecule that enhances the activity of specific immune cells, such as T cells and natural killer (NK) cells, which are essential for cell-mediated immunity. IL-12 stimulates these cells to produce interferon-gamma (IFN-γ), a potent antiviral and antitumor cytokine. Additionally, IL-12 promotes the differentiation of T helper cells into the Th1 subtype, which is involved in coordinating cellular immune responses. |
The IL12RB1 protein solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of phosphate-buffered saline (pH 7.4), 30% glycerol, 1 mM EDTA, and 0.1 mM PMSF.
The purity of the IL12RB1 protein is greater than 85%, as determined by SDS-PAGE analysis.
Interleukin 12 Receptor Beta 1 (IL-12Rβ1) is a crucial component of the immune system, playing a significant role in the signaling pathways of interleukin-12 (IL-12) and interleukin-23 (IL-23). This receptor is essential for the activation and differentiation of T cells and natural killer (NK) cells, which are vital for the body’s defense against infections and cancer.
IL-12Rβ1 is a glycoprotein that forms part of the IL-12 receptor complex. It binds to IL-12 with low affinity and, in association with IL-12Rβ2, forms a high-affinity receptor for IL-12 . This receptor complex is involved in the signal transduction pathways that lead to the activation of Janus family tyrosine kinase 2 (JAK2) and signal transducer and activator of transcription 4 (STAT4), which are critical for the immune response .
The structure of IL-12Rβ1 has been elucidated through various techniques, including X-ray crystallography and cryoelectron microscopy. These studies have revealed the detailed interactions between IL-12Rβ1 and its ligands, providing insights into its function and potential therapeutic targeting .
The recombinant production of IL-12Rβ1 in Sf9 cells involves the use of the baculovirus expression vector system (BEVS). Sf9 cells, derived from the ovarian tissue of the fall armyworm (Spodoptera frugiperda), are commonly used for this purpose due to their ability to produce high yields of recombinant proteins . These cells can be cultured in suspension or as adherent cultures and can grow in serum-free media, making them suitable for large-scale protein production .
The process begins with the insertion of the IL-12Rβ1 gene into the baculovirus genome, which is then used to infect Sf9 cells. The infected cells produce the recombinant IL-12Rβ1 protein, which can be harvested and purified for research and therapeutic applications .
Recombinant IL-12Rβ1 produced in Sf9 cells is used in various research and clinical applications. It is instrumental in studying the signaling pathways of IL-12 and IL-23, which are involved in immune responses against pathogens and tumors . Additionally, understanding the structure and function of IL-12Rβ1 can aid in the development of targeted therapies for autoimmune diseases and cancers .
The ability to produce recombinant IL-12Rβ1 in large quantities also facilitates the development of diagnostic tools and therapeutic agents. For instance, IL-12Rβ1 can be used to screen for potential inhibitors that may modulate the immune response, providing new avenues for treating inflammatory and autoimmune conditions .