Recombinant Human Interleukin-15 receptor subunit alpha (IL15RA), partial (Active)

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Code CSB-MP614402HUd7
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Size $124
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Activity
    Measured by its binding ability in a functional ELISA. Immobilized Human IL15RA at 2 μg/ml can bind Human IL15(CSB-MP011593HU).The EC50 is 32.53-38.41 ng/mL. Biological Activity Assay
  • The purity of IL15RA was greater than 95% as determined by SEC-HPLC
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Greater than 95% as determined by SEC-HPLC.
Activity
Measured by its binding ability in a functional ELISA. Immobilized Human IL15RA at 2 μg/mL can bind Human IL15(CSB-MP011593HU).The EC50 is 32.53-38.41 ng/mL.
Target Names
Uniprot No.
Alternative Names
IL-15 receptor subunit alpha; IL-15R-alpha; IL-15RA
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
31-205aa
Target Protein Sequence
ITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSS
Mol. Weight
24.9 kDa
Protein Length
Partial
Tag Info
C-terminal 10xHis-tagged
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, pH 7.4
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The recombinant human IL15RA protein, an active form of the interleukin-15 receptor alpha (31- 205aa), is produced with a high purity level exceeding 95%, as confirmed by both SDS-PAGE and SEC-HPLC methods. This high purity is crucial as it minimizes contaminants that could potentially interfere with biological activity, ensuring reliable experimental outcomes. This recombinant IL15RA protein is expressed in mammalian cells. It exhibits significant biological activity, which is measured through its binding capacity in a functional ELISA. Specifically, when immobilized at a concentration of 2 μg/mL, IL15RA can effectively bind to human IL15, with an EC50 value ranging from 32.53 to 38.41 ng/mL. This indicates a strong interaction between IL15RA and its ligand, which is essential for its role in immune response modulation.

The IL15RA protein plays a crucial role in the immune response as a component of the IL-15 signaling pathway. IL15RA primarily binds IL-15, a cytokine essential for regulating and activating T cells, natural killer (NK) cells, and other immune cells. It can function in both cis and trans configurations, enhancing IL-15 signaling by presenting the cytokine to neighboring cells and facilitating the activation of intracellular signaling pathways, including the Jak-STAT and PI3K/AKT pathways [1][2].

The presence of IL15RA is often associated with enhanced cell proliferation and survival. Studies indicate that increased expression of IL15RA leads to augmented Jak-STAT signaling, which is critical for the growth and maintenance of T and NK cells [3][4]. Furthermore, the receptor has been shown to inhibit apoptotic pathways, contributing to the persistence of immune cells during immune responses [3][5][4]. A notable feature of IL15RA is its ability to form complexes with other receptor components, such as the beta and gamma chains, which may further amplify the IL-15-mediated signaling cascade [1].

Moreover, IL15RA has significant implications in various pathological contexts, including cancer and chronic inflammatory diseases. Elevated levels of IL15RA and its cognate cytokine can contribute to cancer progression by promoting tumor survival and immune evasion mechanisms [6][7]. In chronic inflammatory conditions, soluble forms of IL15RA can act as antagonists to IL-15, modulating inflammatory responses [4][8]. This duality in function indicates that IL15RA not only promotes immune activation but also serves regulatory roles in preventing excessive inflammation.

Recent findings have also connected IL15RA to specific populations of immune cells, such as Th17 cells, which are implicated in diseases like inflammatory bowel disease (IBD) [6]. The dynamic expression and functional state of IL15RA indicate its essential role in standard immune responses and mediating responses in pathological conditions characterized by dysregulation of immune function [9].

References:
[1] C. Sun, C. Liu, et al. Causal relationship between circulating cytokines and follicular lymphoma: a two-sample mendelian randomization study. Am J Cancer Res, vol. 14, no. 4, p. 1577-1593, 2024. https://doi.org/10.62347/jckd6973
[2] C. Ratthé and D. Girard. Interleukin-15 enhances human neutrophil phagocytosis by a syk-dependent mechanism: importance of the il-15rα chain. Journal of Leukocyte Biology, vol. 76, no. 1, p. 162-168, 2004. https://doi.org/10.1189/jlb.0605298
[3] Y. Liu, F. Teng, et al. An integrative pharmacogenomic approach identifies two-drug combination therapies for personalized cancer medicine. Scientific Reports, vol. 6, no. 1, 2016. https://doi.org/10.1038/srep22120
[4] E. Mortier, J. Bernard, A. Plet, & Y. Jacques. Natural, proteolytic release of a soluble form of human il-15 receptor α-chain that behaves as a specific, high affinity il-15 antagonist. The Journal of Immunology, vol. 173, no. 3, p. 1681-1688, 2004. https://doi.org/10.4049/jimmunol.173.3.1681
[5] Q. Guo, S. Lv, S. Wu, X. Tian, & Z. Li. Association between single nucleotide polymorphism of il15ra gene with susceptibility to ossification of the posterior longitudinal ligament of the spine. Journal of Orthopaedic Surgery and Research, vol. 9, no. 1, 2014. https://doi.org/10.1186/s13018-014-0103-6
[6] J. Golob, G. Hou, et al. Il-15 promotes inflammatory th17 cells in the intestine. 2023. https://doi.org/10.1101/2023.03.11.532227
[7] P. Marra, S. Mathew, et al. Il15ra drives antagonistic mechanisms of cancer development and immune control in lymphocyte-enriched triple-negative breast cancers. Cancer Research, vol. 74, no. 17, p. 4908-4921, 2014. https://doi.org/10.1158/0008-5472.can-14-0637
[8] E. Mortier, A. Quéméner, et al. Soluble interleukin-15 receptor α (il-15rα)-sushi as a selective and potent agonist of il-15 action through il-15rβ/γ. Journal of Biological Chemistry, vol. 281, no. 3, p. 1612-1619, 2006. https://doi.org/10.1074/jbc.m508624200
[9] J. Gygi, C. Maguire, et al. Integrated longitudinal multiomics study identifies immune programs associated with acute covid-19 severity and mortality. Journal of Clinical Investigation, vol. 134, no. 9, 2024. https://doi.org/10.1172/jci176640

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Target Background

Function
High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. In neutrophils, binds and activates kinase SYK in response to IL15 stimulation. In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner. Expression of different isoforms may alter or interfere with signal transduction.; Does not bind IL15.; Does not bind IL15.; Does not bind IL15.; Does not bind IL15.
Gene References into Functions
  1. Men with the IL-15Ralpha 1775AA genotype spent more time in light intensity physical activity (39.4 +/- 2.4 hr/week) than men with the CC genotype (28.6 +/- 2.3 hr/week, (p = .009). PMID: 29624921
  2. this study describes variants of splicing of IL-15Ra expressed in intestinal epithelial cells, and identifies those variants with the ability of binding IL-15 and following the secretory pathway, as well as determines if any of these variants are regulated by methylation of DNA PMID: 27794069
  3. significant association of rs2228059 with ossification of the posterior longitudinal ligament of the spine in Chinese Han population PMID: 25387549
  4. Report Il15Ralpha levels in synovial fluid from rheumatoid arthritis patients. PMID: 25879761
  5. NK cell activation in human hantavirus infection explained by virus-induced IL-15/IL15Ralpha expression PMID: 25412359
  6. Coexpression of IL15RA and IL15 was also sufficient to activate peripheral blood mononuclear cells. PMID: 24980552
  7. our study provides strong evidence that the functional IL-15RA rs2228059 A>C polymorphism may contribute to the risk of ESCC. PMID: 24464181
  8. We show that a gene transfer approach using recombinant adenovirus to express IL-15 and IL-15Ralpha in murine TRAMP-C2 prostate or TS/A breast tumors induced antitumor immune responses PMID: 24572789
  9. This present study demonstrated that IL15RA rs2228059 A > C polymorphism might modify Gastric cardiac adenocarcinoma susceptibility PMID: 24696261
  10. The proportion of IL-15Ralpha expression on total leukocytes was much lower for all rheumatic diseases, including Behcet disease, than in healthy controls PMID: 23417200
  11. Single nucleotide polymorphism in IL15RA gene is associated with ER-positive breast cancers only in American women of African ancestry. PMID: 23996684
  12. lower frequencies of IL-15RA-positive T cells in Behcet's disease PMID: 23618691
  13. Epidermal IL-15Ralpha acts as an endogenous antagonist of psoriasiform inflammation in mouse and man. PMID: 24019554
  14. The inflammatory bowel diseases patients have an increased expression of IL-15Ralpha mRNA in the mucosa; expression is localized in B cells, suggesting that IL-15 regulates B-cell functions during bowel inflammation. PMID: 23039249
  15. The expression of IL-15Ralpha on CD8 T cells is required for uncontrolled aggressive lymphoproliferation; none of the IL-15Ralpha(-/-)-IL-15 mice that we followed for more than 2 years developed the fatal disease despite controlled expansion of CD8 T cells PMID: 21304101
  16. IL-15 is produced and secreted only as a heterodimer with IL-15Ralpha. PMID: 22496150
  17. High serum IL-15R alpha is associated with T-cell large granular lymphocyte leukemia. PMID: 22049515
  18. These results suggest that IL15RA polymorphism may be associated with the susceptibility of ossification of the posterior longitudinal ligament in Korean population. PMID: 21689944
  19. Different levels of IL-15 trans-presentation are required for different natural killer (NK) cell developmental events to reach full maturation status PMID: 21715685
  20. broad expression pattern of functional IL-15RA splicing forms and suggests a regulatory role of DNA methylation in IL-15RA transcript Var1 expression in mononuclear cells PMID: 21097393
  21. mRNA for IL-15 receptor alpha was constitutively expressed in all tested human fetal brain structures, indicating a role in their development and physiology PMID: 12114302
  22. interleukin-15alpha receptor binds to IL-15 at specific binding sites, one in the B helix and the other in the C helix PMID: 15039446
  23. Soluble IL-15R alpha arises from proteolytic shedding of the membrane-anchored receptor. It is an inhibitor of IL-15 binding to the membrane receptor & of IL-15-induced cell proliferation. IL-15R alpha shedding may have major immunoregulatory functions. PMID: 15265897
  24. IL-15 is an important mediator of muscle mass response to resistance exercise training in humans and that genetic variation in IL15RA accounts for a significant proportion of the variability in this response. PMID: 15531573
  25. Study of three-dimensional structure of IL-15 receptor (IL-15R) alpha chain has led to a model of the IL-15.IL-15R alpha complex that reveals involvement of a large network of ionic interactions not observed in other cytokine/cytokine receptor complexes. PMID: 16377614
  26. Results show that the biological activity of soluble IL-15 is much improved after interaction with recombinant soluble IL-15Ralpha. PMID: 16757567
  27. Data show that NK cell survival mediated through the regulatory synapse with human dendritic cells requires IL-15Ralpha. PMID: 17948125
  28. sIL-15Ralpha has a protumor role in cancer PMID: 18483276
  29. genetic variability of the IL-15 receptor has an important role in body fat composition. PMID: 19309557
  30. IL-15 receptor alpha facilitates the stability and secretion of the IL-15 short signal peptide, a soluble and bioactive isoform. PMID: 19696432

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Subcellular Location
Membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Cell surface. Note=Mainly found associated with the nuclear membrane.; [Isoform 5]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane.; [Isoform 6]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane.; [Isoform 7]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane.; [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane.; [Soluble interleukin-15 receptor subunit alpha]: Secreted, extracellular space.
Tissue Specificity
Expressed in neutrophils (at protein level). Expressed in fetal brain with higher expression in the hippocampus and cerebellum than in cortex and thalamus. Higher levels of soluble sIL-15RA form in comparison with membrane-bound forms is present in all br
Database Links

HGNC: 5978

OMIM: 601070

KEGG: hsa:3601

STRING: 9606.ENSP00000369312

UniGene: Hs.445124

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