Interleukin 2 receptor subunit beta, IL2RB, CD122, IL15RB, P70-75, IL-2R subunit beta.
Greater than 95.0% as determined by SDS-PAGE.
IL2RB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-240 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 220 amino acids and having a molecular mass of 25.5kDa.IL2RB shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
The interleukin 2 receptor (IL2R) is a protein crucial for T cell-mediated immune responses. The IL2R interacts with IL2 in three forms, each with a different binding affinity. The alpha subunit monomer (CD25) has the lowest affinity and doesn't participate in signal transduction. The highest affinity form comprises three subunits (alpha/beta/gamma), forming a heterotrimer. The intermediate affinity form consists of a heterodimer of gamma/beta subunits. Both the high and intermediate affinity forms are involved in IL2-induced receptor-mediated endocytosis and the transduction of mitogenic signals.
IL2RB, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain encompassing amino acids 27-240. It's fused to a 6 amino acid His Tag at the C-terminus, resulting in a total of 220 amino acids and a molecular mass of 25.5kDa. Under reducing conditions on SDS-PAGE, IL2RB displays multiple bands ranging from 28-40kDa. Its purification is achieved through proprietary chromatographic techniques.
The IL2RB protein solution is provided at a concentration of 0.25mg/ml. It's formulated in Phosphate Buffered Saline (pH 7.4) and contains 10% glycerol.
The purity of the protein is determined to be greater than 95% using SDS-PAGE analysis.
Interleukin 2 receptor subunit beta, IL2RB, CD122, IL15RB, P70-75, IL-2R subunit beta.
AVNGTSQFTC FYNSRANISC VWSQDGALQD TSCQVHAWPD RRRWNQTCEL LPVSQASWAC NLILGAPDSQ KLTTVDIVTL RVLCREGVRW RVMAIQDFKP FENLRLMAPI SLQVVHVETH RCNISWEISQ ASHYFERHLE FEARTLSPGH TWEEAPLLTL KQKQEWICLE TLTPDTQYEF QVRVKPLQGE FTTWSPWSQP LAFRTKPAAL GKDTHHHHHH.
IL-2Rβ is a transmembrane protein that spans the cell membrane and is involved in the high-affinity binding of IL-2. The binding of IL-2 to its receptor triggers a cascade of intracellular signaling pathways, including the JAK-STAT pathway, which leads to the activation of various genes involved in immune responses . The IL-2Rβ subunit is particularly important for the activation of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs), which are essential for the body’s defense against infections and cancer .
Recombinant human IL-2Rβ is produced using advanced biotechnological methods, typically involving the expression of the IL-2Rβ gene in host cells such as Escherichia coli or Pichia pastoris. This recombinant protein is used in various research and therapeutic applications, including the study of immune responses and the development of cancer immunotherapies .
Recombinant IL-2Rβ has been explored for its potential in cancer immunotherapy. By enhancing the activity of IL-2, researchers aim to boost the immune system’s ability to target and destroy cancer cells. However, the clinical use of IL-2 has been limited by its short half-life and the potential for severe side effects, such as cytokine release syndrome and vascular leak syndrome . To overcome these challenges, scientists have developed modified versions of IL-2 and IL-2Rβ that have improved pharmacokinetic properties and reduced toxicity .
Recent advancements in the field have led to the development of long-acting IL-2 variants and IL-2Rβ-selective agonists. These novel therapeutics are designed to selectively activate immune cells that express IL-2Rβ while minimizing the activation of regulatory T cells (Tregs) and other cells that may contribute to adverse effects . Preclinical studies have shown promising results, with these new agents demonstrating enhanced anti-tumor activity and improved safety profiles.