Mouse IL-15 R alpha PerCP-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: IL-15R alpha

IL-15R alpha (also known as CD215) is a unique, 52-55 kDa Sushi domain-containing protein that is produced by a wide variety of cell types. Mouse IL-15 R alpha is a type I transmembrane glycoprotein that contains a 173 amino acid (aa) extracellular region (aa 33-205) coupled to a short 37 aa cytoplasmic tail. It is found on a wide variety of cells, including hepatocytes, keratinocytes, B cells, T cells, intestinal columnar epithelium, macrophages, dendritic cells and select fibroblasts. IL-15 R alpha binds soluble, 15-19 kDa monomeric IL-15 with high affinity, and effectively and serves as a heterodimeric partner for the cytokine. Most (if not all) effects attributable to IL-15 are mediated by the heterodimeric IL-15:IL-15 R alpha complex that binds to two signaling subunits, the 72-76 kDa IL-2R beta subunit, and the 64-65 kDa common gamma chain ( gamma c). The latter two subunits have a restricted expression pattern and generally relate to hematopoietic cells. The IL-15:IL-15 R alpha complex exists in two forms. The first form finds IL-15 bound to transmembrane IL-15 R alpha, while the second form finds IL-15 bound to soluble IL-15 R alpha, a product of proteolytic cleavage. This soluble complex may exist as a 140-160 kDa heteromultimer. Functionally, the transmembrane IL-15:IL-15 R alpha complex appears to be the most important. Typically, IL-15 binds transmembrane IL-15 R alpha in the ER, and this complex is then presented on the cell surface where it acts in-trans on adjacent IL-2R beta : gamma c expressing cells. Alternatively, the IL-15:IL-15 R alpha complex may also act in-cis, particularly on hematopoietic (or T) cells. In mouse, in-trans presentation is considered crucial to IL-15 activity, while the human system appears to utilize both in-trans and in-cis mechanisms. The function of the soluble complex is unclear; on the one hand, its creation via proteolytic cleavage is suggested to act as a neutralizer of IL-15 activity, while on the other hand, it is proposed to serve as a cytokine "hormone" that activates NK and CD8⁺ T cells at distant sites. Mouse IL-15 R alpha has at least five isoform variants, two of which are incapable of binding IL-15. The first isoform shows a Met substitution for aa 1-206. The second isoform utilizes an alternative start site at Met141, precluding the existence of an IL-15 Sushi binding domain over aa 34-98. The remaining three isoforms contain the ligand binding Sushi domain, but exhibit deletions of aa 129-161, aa 129-194, and aa 98-195. On balance, the IL-15:IL-15 R alpha system is considered crucial for generating and maintaining central and effector memory CD8⁺ T cells, NK cells and NKT cells. Over aa 33-205, mouse IL-15 R alpha shares 89% and 59% aa sequence identity with rat and human IL-15 R alpha, respectively.  

Product Datasheets

Related Research Areas

• Common gamma Chain Receptor Family
• Cytokine and Growth Factor Receptors on VSMC
• Group 1 ILCs
• Isolation, Culture, and Identification of Natural Killer Cells
• Natural Killer T (NKT) Cells
• Receptors in the Jak/STAT Pathway