Interleukin 15 Receptor Subunit Alpha, Interleukin 15 Receptor, Alpha, Interleukin 15 Receptor Alpha Isoform EM2, Interleukin 15 Receptor Alpha Isoform IC2, Interleukin 15 Receptor Alpha Isoform IC3, Interleukin 15 Receptor Alpha Isoform IC4, Interleukin 15 Receptor Alpha Isoform IC5, Interleukin 15 Receptor Alpha Isoform IC6, Interleukin 15 Receptor Alpha Isoform IC7,Interleukin 15 Receptor Alpha Isoform IC8, Interleukin-15 Receptor Subunit Alpha, IL-15 Receptor Subunit Alpha, CD215 Antigen, IL-15R-Alpha, IL-15RA, CD215.
Greater than 90.0% as determined by SDS-PAGE.
IL15RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (31-205 a.a.) and fused to a 242 a.a. hIgG-His Tag at C-terminus containing a total of 417 amino acids and having a molecular mass of 45.6kDa.
IL15RA shows multiple bands between 57-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
IL15RA, also called Interleukin 15 Receptor Alpha, is a receptor that binds with high affinity to interleukin-15. It forms a heterotrimer with the beta and gamma subunits of the IL-2 receptor in order to initiate signal transduction. IL15/IL15R alpha complexes have the capacity to transmit reverse signaling, which in turn stimulates cellular adhesion, the addition of phosphate groups to tyrosine residues on intracellular proteins, and the release of cytokines by the IL-15/IL15R alpha expressing cells.
IL15RA, as produced in Sf9 Baculovirus cells, is a single polypeptide chain that has been glycosylated. It consists of amino acids 31-205 and is fused at its C-terminus to a 242 amino acid hIgG-His Tag. This results in a protein with a total of 417 amino acids and a molecular weight of 45.6kDa.
When subjected to SDS-PAGE under reducing conditions, IL15RA exhibits multiple bands with molecular weights ranging from 57-70kDa. It is purified using proprietary chromatographic techniques.
The IL15RA protein solution is provided at a concentration of 0.5mg/ml and is prepared in a buffer containing phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity levels exceed 90.0%, as determined by SDS-PAGE analysis.
Biological activity is assessed based on the protein's ability to suppress the proliferation of CTLL2 mouse cytotoxic T cells. The ED50, which represents the effective concentration required to inhibit proliferation by 50%, is less than 2 ng/ml in the presence of Human IL-15.
Interleukin 15 Receptor Subunit Alpha, Interleukin 15 Receptor, Alpha, Interleukin 15 Receptor Alpha Isoform EM2, Interleukin 15 Receptor Alpha Isoform IC2, Interleukin 15 Receptor Alpha Isoform IC3, Interleukin 15 Receptor Alpha Isoform IC4, Interleukin 15 Receptor Alpha Isoform IC5, Interleukin 15 Receptor Alpha Isoform IC6, Interleukin 15 Receptor Alpha Isoform IC7,Interleukin 15 Receptor Alpha Isoform IC8, Interleukin-15 Receptor Subunit Alpha, IL-15 Receptor Subunit Alpha, CD215 Antigen, IL-15R-Alpha, IL-15RA, CD215.
ADPITCPPPM SVEHADIWVK SYSLYSRERY ICNSGFKRKA GTSSLTECVL NKATNVAHWT TPSLKCIRDP ALVHQRPAPP STVTTAGVTP QPESLSPSGK EPAASSPSSN NTAATTAAIV PGSQLMPSKS PSTGTTEISS HESSHGTPSQ TTAKNWELTA SASHQPPGVY PQGHSDTTLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH
Interleukin 15 Receptor Alpha (IL-15Rα) is a protein that plays a crucial role in the immune system by binding to interleukin 15 (IL-15) with high affinity. This receptor is part of the cytokine receptor family and is involved in various immune responses, including the proliferation and activation of natural killer (NK) cells and T cells. Recombinant human IL-15Rα is a laboratory-produced version of this receptor, used in research and therapeutic applications.
IL-15Rα is a high-affinity receptor for IL-15, a cytokine that shares many biological activities with interleukin 2 (IL-2). The receptor is structurally related to IL-2Rα but has distinct roles. Unlike IL-2Rα, IL-15Rα can bind IL-15 independently of other subunits, which suggests unique functions for IL-15 in the immune system .
The receptor is composed of several domains, including the sushi domain, which is crucial for its high-affinity binding to IL-15. The recombinant form of IL-15Rα often includes the extracellular sushi domain, which maintains the natural biological effect of the receptor .
IL-15Rα is involved in various immune responses. It enhances cell proliferation and the expression of apoptosis inhibitors such as BCL2L1/BCL2-XL and BCL2. This receptor is also essential for IL-15-induced phagocytosis in neutrophils, a process dependent on the kinase SYK .
IL-15 and its receptor play a significant role in both innate and adaptive immunity. IL-15 is constitutively expressed by a wide range of cell types, including monocytes, macrophages, dendritic cells, keratinocytes, fibroblasts, myocytes, and nerve cells. This cytokine is crucial for the proliferation of NK cells and the activation of T cells, making it a vital component of the immune response .
Recombinant human IL-15Rα is produced using various biotechnological methods to study its function and potential therapeutic applications. The recombinant form is often used in research to understand the receptor’s role in immune responses and to develop new treatments for diseases involving the immune system.
One common form of recombinant IL-15Rα is the soluble sushi domain, which includes the extracellular domain of the receptor. This form is a high-affinity agonist of IL-15 and is used in culture to maintain the natural biological effects of the receptor . Another form is the Fc fusion protein, which combines the extracellular domain of IL-15Rα with the Fc portion of human IgG. This fusion protein has a calculated molecular weight of 44.4 kDa and is used in various research applications .
The unique properties of IL-15Rα make it a promising target for therapeutic interventions. By modulating the activity of IL-15, researchers aim to develop treatments for various immune-related disorders, including cancer, autoimmune diseases, and infectious diseases. The recombinant forms of IL-15Rα are valuable tools in these efforts, providing insights into the receptor’s function and potential therapeutic applications.