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Biotinylated Human IL-15RA&IL-15 Protein (Primary Amine Labeling) 3366

$525.00$1,750.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Ile31-Ser108 (IL-15RA) & Asn49-Ser162 (IL-15)
SKU: 3366parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE

background

Interleukin-15 receptor alpha (IL-15R alpha) is a high affinity IL-15 binding protein that is crucial for mediating IL-15 functions such as memory CD8 T cell proliferation and NK, NK/T cell, and intestinal intraepithelial lymphocyte development.

molecular weight

The protein has a predicted MW of 23.8 kDa. Due to glycosylation, the protein migrates to 25-28 kDa&30-35 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1 EU per ug by the LAL method.

Biotinylated Human IL-15RA&IL-15 Protein (Primary Amine Labeling) 3366

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
Interleukin-15 receptor alpha (IL-15R alpha) is a high affinity IL-15 binding protein that is crucial for mediating IL-15 functions such as memory CD8 T cell proliferation and NK, NK/T cell, and intestinal intraepithelial lymphocyte development.
Protein names
Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)]
Gene names
IL15RA,IL15RA
Mass
28233Da
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]: Does not bind IL15.; [Isoform 6]: Does not bind IL15.; [Isoform 7]: Does not bind IL15.; [Isoform 8]: Does not bind IL15.
Subellular 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 .
Tissues
Expressed in neutrophils (at protein level) (PubMed:15123770). Expressed in fetal brain with higher expression in the hippocampus and cerebellum than in cortex and thalamus (PubMed:12114302). Higher levels of soluble sIL-15RA form in comparison with membrane-bound forms is present in all brain structures (PubMed:12114302). Isoforms 1, 3, 4, 5, 6, 7, 8 and 9: Widely expressed (PubMed:10480910, PubMed:8530383).
Structure
The interleukin-15 receptor IL15R is a heterotrimer of IL15RA, IL2RB and IL2RG. IL15RA also self-associates (PubMed:17643103). Interacts with SYK (PubMed:15123770).
Post-translational modification
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).
Target Relevance information above includes information from UniProt accession: Q13261
The UniProt Consortium

Data

ELISA with Biotinylated Human IL-15RA&IL-15 Protein (Primary Amine Labe
Immobilized Human IL-2 R beta, hFc Tag at 1 µg/ml (100 µl/Well) on the plate. Dose response curve for Biotinylated Human IL-15Ra&IL-15, His Tag with the EC50 of 18.5 ng/ml determined by ELISA.
SDS-PAGE gel of Biotinylated Human IL-15RA&IL-15 Protein (Primary Amine
Biotinylated Human IL-15RA&IL-15 (Primary Amine Labeling) on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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Protocols

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Documents

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