IL21R Mouse

Interleukin-21 (IL-21) is a cytokine primarily produced by activated CD4+ T cells that plays a crucial role in regulating immune responses. It exerts its effects by binding to the IL-21 receptor (IL-21R), a heterodimeric receptor complex expressed on various immune cells, including B cells, T cells, and natural killer (NK) cells. IL-21 binding to its receptor initiates intracellular signaling cascades, leading to the activation of downstream signaling pathways, such as JAK/STAT pathway, ultimately influencing cell proliferation, differentiation, and effector functions. IL-21 exhibits pleiotropic effects on both innate and adaptive immune responses. It is involved in the differentiation of B cells into antibody-producing plasma cells, enhances antibody production, and supports the development of memory B cells, thereby contributing to humoral immunity. IL-21 also promotes the cytotoxic activity of CD8+ T cells and NK cells, enhancing their ability to eliminate virus-infected cells and tumor cells. Moreover, IL-21 plays a role in regulating T cell differentiation and function, influencing the balance between effector and regulatory T cell subsets. Given its multifaceted roles in immune regulation, IL-21 has been implicated in the pathogenesis of various autoimmune diseases, inflammatory disorders, and cancers. Targeting IL-21 or its receptor has emerged as a potential therapeutic strategy for modulating immune responses in these conditions.

IL-21R Mouse Recombinant is a genetically engineered protein produced in HEK293 cells, a human embryonic kidney cell line widely used for protein expression. This recombinant protein consists of the extracellular domain of mouse IL-21R fused to a human IgG-His-Tag at the C-terminus. The extracellular domain of IL-21R is responsible for binding to IL-21, while the human IgG-His-Tag facilitates protein purification and detection. The protein has a molecular weight of approximately 52 kDa, and it appears as a colorless solution after sterile filtration. The purity of the protein is greater than 95% as determined by SDS-PAGE analysis.

Sterile, clear, and colorless solution.

The IL21R protein solution is provided at a concentration of 0.25 mg/ml in a buffer containing phosphate-buffered saline (PBS) at pH 7.4 and 10% glycerol. PBS provides a physiologically relevant pH and salt concentration, while glycerol acts as a cryoprotectant, preventing protein degradation during freezing and thawing.

For short-term storage (up to 4 weeks), the IL21R solution should be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. To ensure optimal stability during long-term storage, it is advisable to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to the solution. Carrier proteins help to prevent protein aggregation and degradation. It is crucial to avoid repeated freezing and thawing of the IL21R solution, as this can lead to protein denaturation and loss of activity.

The purity of the IL21R Mouse Recombinant protein is greater than 95%, as determined by SDS-PAGE analysis. This high level of purity ensures the reliability and consistency of experimental results.

The biological activity of the IL21R Mouse Recombinant protein is measured by its ability to inhibit interferon-gamma (IFN-γ) secretion by NK-92 human natural killer cells in the presence of mouse IL-2. The ED50 value, which represents the effective dose of the protein required to inhibit IFN-γ secretion by 50%, is less than or equal to 4 µg/ml. This assay demonstrates the functional activity of the recombinant IL21R protein in inhibiting IL-21 signaling.

Interleukin-21 receptor, IL-21 receptor, IL-21R, Il21r, Lymphocyte receptor beta, LR-beta, Novel interleukin receptor, Novel cytokine receptor 8, NR8, Novel interleukin receptor, CD360, CD360 antigen, NILR, Nilr.

HEK293 Cells.

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