IL-15R alpha Protein, Mouse (HEK293, hFc)
Based on 1 Customer Validation
IL-15R alpha is a high affinity receptor for IL-15 (Kd: 100 pM). IL-15R alpha binds IL-15 and thereby activating the antitumor functions of NK cells and CD8+ T cells. IL-15R alpha plays an important role in memory CD8+ T cell homeostasis and lymphocyte development. IL-15R alpha Protein, Mouse (HEK293, hFc) is a recombinant mouse extracellular region of IL-15R alpha (G33-K205) with a C-Terminal hFc tag, which is produced in HEK293 cells.
- Species: Mouse
- Source: HEK293
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
IL-15R alpha is a high affinity receptor for IL-15 (Kd: 100 pM)[1]. IL-15R alpha binds IL-15 and thereby activating the antitumor functions of NK cells and CD8+ T cells[2]. IL-15R alpha plays an important role in memory CD8+ T cell homeostasis and lymphocyte development[3]. IL-15R alpha Protein, Mouse (HEK293, hFc) is a recombinant mouse extracellular region of IL-15R alpha (G33-K205) with a C-Terminal hFc tag, which is produced in HEK293 cells.
Background
IL-15R alpha is expressed on various cell types, including lymphocytes, myeloid cells, nonlymphoid and nonhematopoietic cells[4]. IL-15R alpha is down-regulated in Epstein-Barr virus associated gastric cancer (EBVaGC) via promoter hypermethylation[5].
The sequence of amino acids in IL-15R alpha differs in different species. Mouse IL-15R alpha shares <55% aa sequence identity with human.
IL-15R alpha is required for transporting of IL-15 from the endoplasmic reticulum to the cell surface to bind with β (CD122) and γ (CD132) chains on responding lymphocytes[4][6]. When binding with IL-15, the complex increases the in vivo half-life of IL-15 and enhances binding affinity of IL-15 with IL-15Rβ/γ in NK cells and CD8+ T cells. Thus, the signal transmission improves proliferation and antitumor activities of NK cells and CD8+ T cells[2]. Moreover, IL-15R alpha on the cancer cell surface induces the malignant phenotype, such as augmented cancer cell growth, migration and invasion, and decreased apoptosis[5]. IL-15R alpha mediates immune responses, and is important for lymphocyte activation and proliferation, NK cell survival and proliferation[7].
IL-15R alpha binds with IL-15 and activates the antitumor functions of NK cells and CD8+ T cells, and is also important in memory CD8 T cell homeostasis and lymphocyte development[2][3].
In Vitro
IL-15R alpha (mouse) exhibits a high level of IL-15 binding with high affinity when transfected to 32D-01 cells[8].
Verified Bioactivity
Measured by its ability to block human IL-15-induced proliferation of CTLL-2 mouse cytotoxic T cells.The ED50 for this effect is <10 ng/mL.
MCE Validation Data
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Purity - SDS-PAGE
Purity - SDS-PAGE
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Bioactivity - Cell-Based Assay
Bioactivity - Cell-Based Assay
Technical Parameters
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Species Mouse
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Source HEK293
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Tag C-hFc
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Accession
Q60819-1 (G33-K205)
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Molecular Construction
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N-term
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IL-15Rα (G33-K205)
Accession # Q60819-1 -
hFc
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C-term
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Protein Length
Extracellular Domain
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Synonyms
IL15RA; IL-15 Receptor Subunit Alpha; Interleukin 15 Receptor Subunit Alpha; IL15RA Protein; Interleukin-15 Receptor Subunit Alpha; CD215 Antigen; IL-15RA; IL-15R-Alpha; CD215; Il15ra; Interleukin 15 Receptor, Alpha
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AA Sequence
GTTCPPPVSIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLIECVINKNTNVAHWTTPSLKCIRDPSLAHYSPVPTVVTPKVTSQPESPSPSAKEPEAFSPKSDTAMTTETAIMPGSRLTPSQTTSAGTTGTGSHKSSRAPSLAATMTLEPTASTSLRITEISPHSSKMTK
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Molecular Weight
Approximately 60-90 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder.
Lyophilized from a 0.2 μm solution of 20 mM PB, 150 mM NaCl, pH 7.4, 8% trehalose.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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Handling Instructions (2659 KB)
References
[1]. Yin Guo, et al. Immunobiology of the IL-15/IL-15Rα complex as an antitumor and antiviral agent. Cytokine Growth Factor Rev. 2017 Dec;38:10-21. [Content Brief]
[2]. Johan Mj Van den Bergh, et al. IL-15 receptor alpha as the magic wand to boost the success of IL-15 antitumor therapies: The upswing of IL-15 transpresentation. Pharmacol Ther. 2017 Feb;170:73-79. [Content Brief]
[3]. Spencer W Stonier, et al. Trans-presentation: a novel mechanism regulating IL-15 delivery and responses. Immunol Lett. 2010 Jan 4;127(2):85-92. [Content Brief]
[4]. Patrick R Burkett, et al. IL-15R alpha expression on CD8+ T cells is dispensable for T cell memory. Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4724-9. [Content Brief]
[5]. Jing Wei, et al. Tumor cell-expressed IL-15Rα drives antagonistic effects on the progression and immune control of gastric cancer and is epigenetically regulated in EBV-positive gastric cancer. Cell Oncol (Dordr). 2020 Dec;43(6):1085-1097. [Content Brief]
[6]. Emanuela Romano, et al. Human Langerhans cells use an IL-15R-α/IL-15/pSTAT5-dependent mechanism to break T-cell tolerance against the self-differentiation tumor antigen WT1. Blood. 2012 May 31;119(22):5182-90. [Content Brief]
[7]. J P Lodolce, et al. IL-15 receptor maintains lymphoid homeostasis by supporting lymphocyte homing and proliferation. Immunity. 1998 Nov;9(5):669-76. [Content Brief]
[8]. J G Giri, et al. Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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