IL-15R alpha Protein, Human (Biotinylated, HEK293, His-Avi)
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, Human (Biotinylated, HEK293, His-Avi) is a biotinylated recombinant human extracellular region of IL-15R alpha (I31-T205) with a C-Terminal His-Avi tag, which is produced in HEK293 cells.
- Species: Human
- 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, Human (Biotinylated, HEK293, His-Avi) is a biotinylated recombinant human extracellular region of IL-15R alpha (I31-T205) with a C-Terminal His-Avi 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. Human IL-15R alpha shares <55% aa sequence identity with mouse.
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 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[7].
Verified Bioactivity
1.Immobilized Human IL-15 at 0.5 μg/mL (100μL/Well) on the plate. Dose response curve for Biotinylated Human IL-15RA His with the EC50 of 18-20 ng/mL determined by ELISA.
2.Immobilized Human IL-15 at 2 μg/mL (100 μL/Well) on the plate. Dose response curve for Biotinylated Human IL-15RA, His Tag with the EC50 of 55.8 ng/mL determined by ELISA.
Technical Parameters
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Species Human
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Source HEK293
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Tag C-Avi;C-8*His
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Accession
Q13261-1 (I31-T205)
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Molecular Construction
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N-term
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IL-15Rα (I31-T205)
Accession # Q13261-1 -
8*His-Avi
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C-term
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Protein Length
Extracellular Domain
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Conjugation
Biotin
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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
ITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTT
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Predicted Molecular Mass
21.3 kDa
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Molecular Weight
Approximately 43-70 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Glycosylation
Yes
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Purity
≥ 95%, as determined by Bis-Tris PAGE.
Product Properties
Lyophilized powder.
1.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
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 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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