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Active Recombinant Human IL15RA protein, Fc/Avi-tagged, Biotinylated

Cat.No. : IL15RA-051H
Product Overview : Biotinylated Recombinant Human IL15RA(Ile31-Thr205) protein, fused to Fc/Avi tag at the C-terminus, was expressed in CHO cells .
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Description : Interleukin 15 Receptor alpha (IL‑15 R alpha ), also known as CD215, is a widely expressed 60-kDa transmembrane glycoprotein that plays an important role in the homeostasis and activation of NK cells and CD8+ memory T cells and participates in the development and function of many other hematopoietic cell types and non‑immune cell types (1‑3). Mature human IL‑15 R alpha consists of a 175 amino acid (aa) extracellular domain (ECD) containing one N‑linked glycosylation site, a 23 aa transmembrane segment, and a 39 aa cytoplasmic tail (4). Within the ECD, human IL‑15 R alpha shares approximately 60% aa sequence identity with mouse and rat IL‑15 R alpha. Alternate splicing of human IL‑15 R alpha generates additional isoforms with variable length deletions in the ECD and/or substitutions in the cytoplasmic domain (4, 5). IL‑15 R alpha binds to Interleukin‑15 with high affinity (6). IL‑15 additionally interacts with lower affinity to a complex of IL‑2 R beta and the common gamma chain ( gamma c) which are also subunits of the IL‑2 receptor complex (7, 8). The use of shared receptor components contributes to the overlapping biological effects of IL‑15 and IL‑2. The dominant mechanism of IL‑15 action is known as transpresentation in which IL‑15/IL‑15 R alpha complexes are expressed on the surface of one cell and interact with complexes of IL‑2 R beta / gamma c on adjacent cells (9). This enables cells to respond to IL‑15 even if they do not express IL‑15 R alpha (10‑12). IL‑15/IL‑15 R alpha complexes can transmit reverse signaling that promotes cellular adhesion, tyrosine phosphorylation of intracellular proteins, and cytokine secretion by the IL‑15/IL‑15 R alpha expressing cells (13, 14). Shed soluble forms of IL‑15 R alpha retain the ability to bind tightly to IL‑15 and can inhibit IL‑15 bioactivity (6, 15, 16). Our Avi-tag Biotinylated Recombinant Human IL‑15 R alpha features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
Source : CHO cells
Species : Human
Tag : Fc/Avi
Predicted N Terminal : Ile31
Form : Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Bio-activity : The biotin to protein ratio is greater than 0.7 as determined by the HABA assay.
Measured by its binding ability in a functional ELISA.
When Biotinylated Recombinant Human IL15RA Fc Chimera Avi-tag is immobilized at 0.5 µg/mL (100 µL/well),
Recombinant Human IL15 binds with an ED50 of 0.02-0.16 ng/mL.
Molecular Mass : 70-80 kDa, under reducing conditions
Protein length : Ile31-Thr205
Endotoxin : <0.10 EU per 1 μg of the protein by the LAL method.
Purity : >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Applications : Binding Activity, Bioactivity
Storage : Use a manual defrost freezer and avoid repeated freeze-thaw cycles.12 months from date of receipt, -20 to -70 °C as supplied.1 month, 2 to 8 °C under sterile conditions after reconstitution.3 months, -20 to -70 °C under sterile conditions after reconstitution.
Reconstitution : Reconstitute at 400 μg/mL in PBS.
Gene Name : IL15RA interleukin 15 receptor, alpha [ Homo sapiens ]
Official Symbol : IL15RA
Synonyms : IL15RA; interleukin 15 receptor, alpha; interleukin-15 receptor subunit alpha; CD215; IL 15RA; MGC104179;
Gene ID : 3601
mRNA Refseq : NM_001243539
Protein Refseq : NP_001230468
MIM : 601070
UniProt ID : Q13261

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (10)

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How does immunoprecipitation validate IL15RA's association with IL2RB? 10/23/2022

Immunoprecipitation validates IL15RA's binding to IL2RB in cells.

What are the applications of CRISPR/Cas9 in studying IL15RA knockout models? 07/08/2021

CRISPR/Cas9 technology aids in generating IL15RA knockout models.

Could you explain the approaches to investigate IL15RA's role in autoimmune diseases? 03/15/2021

Approaches unravel IL15RA's implication in autoimmune disease mechanisms.

What experimental strategies differentiate IL15RA's role in innate and adaptive immunity? 06/17/2020

Methods discern IL15RA's distinct roles in innate and adaptive immunity.

What techniques characterize IL15RA isoform expression in tissues? 06/14/2020

RT-PCR and Western blotting assess IL15RA isoform expression patterns.

How is IL15RA's binding affinity to IL15 measured in vitro? 01/05/2019

Binding affinity of IL15RA to IL15 quantified through surface plasmon resonance.

What methods explore IL15RA's involvement in immune cell proliferation? 11/12/2017

Proliferation assays investigate IL15RA's contribution to immune cell growth.

How is IL15RA's interaction with JAK/STAT pathways analyzed? 11/11/2017

IL15RA's interaction with JAK/STAT pathways probed using immunoblotting.

How do siRNA knockdown experiments reveal IL15RA's role in signaling? 04/20/2017

siRNA knockdown studies unveil IL15RA's impact on downstream signaling.

Can you detail the use of FRET assays to study IL15RA dimerization? 01/09/2017

FRET assays employed to elucidate IL15RA dimerization kinetics.

Customer Reviews (3)

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Reviews
10/29/2020

    Effective in T-cell assays.

    03/10/2018

      High purity levels.

      05/28/2017

        Consistent receptor binding.

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