ELISA with Human IL-15RA/IL-15 R alpha/CD215 Protein 4827

Human IL-15RA/IL-15 R alpha/CD215 Protein 4827

$270.00 – $900.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ile31-Thr205

SKU: 4827parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q13261
express system	HEK293
product tag	C-hFc
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
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 45.1 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human IL-15RA/IL-15 R alpha/CD215 Protein 4827

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 Human IL-15RA/IL-15 R alpha/CD215 Protein

Immobilized Human IL-15, No Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Human IL-15RA, hFc Tag with the EC50 of 30.2ng/ml determined by ELISA.

HPLC of Human IL-15RA/IL-15 R alpha/CD215 Protein

The purity of Human IL-15RA is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human IL-15RA/IL-15 R alpha/CD215 Protein

Human IL-15RA 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.