Human Recombinant IL15RA protein, ECD, hFc Tag (V2LY-0526-LY4761)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
hFc Tag
Protein Construction
This product is Human Recombinant IL15RA protein, ECD, hFc Tag consist of Amino Acid: 31-205 and predicts a molecular mass of 45.22 kDa.
Molecule Mass
45.22 kDa
Protein Domain
ECD
Verified
HPLC
Sequence
Amino Acid: 31-205
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
interleukin 15 receptor subunit alpha
Function
High-affinity receptor for interleukin-15 (PubMed:8530383).

Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (By similarity).

In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (PubMed:15123770).

In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (PubMed:15123770).

Expression of different isoforms may alter or interfere with signal transduction (PubMed:10480910).

Isoform 5&6&7&8:
Does not bind IL15.
Biological Process
Interleukin-15-mediated signaling pathway Source: UniProtKB
Positive regulation of natural killer cell differentiation Source: Ensembl
Positive regulation of phagocytosis Source: UniProtKB
Cellular Location
Nucleus membrane; Membrane; Cell surface. Mainly found associated with the nuclear membrane.
Isoform 5: Golgi apparatus membrane; Endoplasmic reticulum membrane; Cytoplasmic vesicle membrane; Membrane. 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: Golgi apparatus membrane; Endoplasmic reticulum membrane; Cytoplasmic vesicle membrane; Membrane. 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: Golgi apparatus membrane; Endoplasmic reticulum membrane; Cytoplasmic vesicle membrane; Membrane. 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: Golgi apparatus membrane; Endoplasmic reticulum membrane; Cytoplasmic vesicle membrane; Membrane. 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: Extracellular space
Topology
Extracellular: 31-205
Helical: 206-228
Cytoplasmic: 229-267
PTM
N-glycosylated and O-glycosylated.
A soluble form (sIL-15RA) arises from proteolytic shedding of the membrane-anchored receptor (PubMed:15265897). It also binds IL-15 and thus interferes with IL-15 binding to the membrane receptor (PubMed:15265897).

Liu, Z., Zou, W., Xu, Y., & Wu, P. (2023). Clinical characterization and immunosuppressive regulation of IL15RA in Kidney renal papillary cell carcinoma through 324 samples.

Fu, S., Kundranda, M. N., Rahimian, S., Shen, Y., Tan, Q., Zhao, R., ... & Liang, T. (2023). The initial report of phase I trial of VG2025, a non-attenuated HSV-1 oncolytic virus expressing IL-12 and IL-15/RA payloads, in patients with advanced solid tumors.

Bellón, T., González-Valle, O., Sendagorta, E., Lerma, V., Martínez del Río, J., Martínez, C., ... & de Abajo, F. (2022). IL-15/IL-15Rα in SJS/TEN: Relevant Expression of IL15 and IL15RA in Affected Skin. Biomedicines, 10(8), 1868.

De Mattia, E., Polesel, J., Roncato, R., Labriet, A., Bignucolo, A., Gagno, S., ... & Toffoli, G. (2021). IL15RA and SMAD3 genetic variants predict overall survival in metastatic colorectal cancer patients treated with folfiri therapy: A new paradigm. Cancers, 13(7), 1705.

Warner, S. C., Nair, A., Marpadga, R., Chubinskaya, S., Doherty, M., Valdes, A. M., & Scanzello, C. R. (2020). IL-15 and IL15RA in osteoarthritis: association with symptoms and protease production, but not structural severity. Frontiers in immunology, 11, 1385.

Yang, H., Zhou, L., Chen, J., Su, J., Shen, W., Liu, B., ... & Qian, J. (2019). A four‑gene signature for prognosis in breast cancer patients with hypermethylated IL15RA. Oncology Letters, 17(5), 4245-4254.

Loro, E., Bisetto, S., & Khurana, T. S. (2018). Mitochondrial ultrastructural adaptations in fast muscles of mice lacking IL15RA. Journal of Cell Science, 131(21), jcs218313.

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For research use only. Not intended for any clinical use.

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