Recombinant Human Interleukin-15 Receptor Subunit Alpha (IL15RA) Protein (hFc)

Name: Recombinant Human Interleukin-15 Receptor Subunit Alpha (IL15RA) Protein (hFc)
Brand: Beta LifeScience
SKU: BLC-06318P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Price Save $107

Size

100ug

Product Overview

Description	Recombinant Human Interleukin-15 Receptor Subunit Alpha (IL15RA) Protein (hFc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q13261
Target Symbol	IL15RA
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-hFc
Target Protein Sequence	ITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTT
Expression Range	31-205aa
Protein Length	Partial
Mol. Weight	47.3 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. In neutrophils, binds and activates kinase SYK in response to IL15 stimulation. In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner. Expression of different isoforms may alter or interfere with signal transduction.; Does not bind IL15.; Does not bind IL15.; Does not bind IL15.; Does not bind IL15.
Subcellular 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.
Database References	HGNC: 5978 OMIM: 601070 KEGG: hsa:3601 STRING: 9606.ENSP00000369312 UniGene: Hs.445124
Tissue Specificity	Expressed in neutrophils (at protein level). Expressed in fetal brain with higher expression in the hippocampus and cerebellum than in cortex and thalamus. Higher levels of soluble sIL-15RA form in comparison with membrane-bound forms is present in all br

Gene Functions References

Men with the IL-15Ralpha 1775AA genotype spent more time in light intensity physical activity (39.4 +/- 2.4 hr/week) than men with the CC genotype (28.6 +/- 2.3 hr/week, (p = .009). PMID: 29624921
this study describes variants of splicing of IL-15Ra expressed in intestinal epithelial cells, and identifies those variants with the ability of binding IL-15 and following the secretory pathway, as well as determines if any of these variants are regulated by methylation of DNA PMID: 27794069
significant association of rs2228059 with ossification of the posterior longitudinal ligament of the spine in Chinese Han population PMID: 25387549
Report Il15Ralpha levels in synovial fluid from rheumatoid arthritis patients. PMID: 25879761
NK cell activation in human hantavirus infection explained by virus-induced IL-15/IL15Ralpha expression PMID: 25412359
Coexpression of IL15RA and IL15 was also sufficient to activate peripheral blood mononuclear cells. PMID: 24980552
our study provides strong evidence that the functional IL-15RA rs2228059 A>C polymorphism may contribute to the risk of ESCC. PMID: 24464181
We show that a gene transfer approach using recombinant adenovirus to express IL-15 and IL-15Ralpha in murine TRAMP-C2 prostate or TS/A breast tumors induced antitumor immune responses PMID: 24572789
This present study demonstrated that IL15RA rs2228059 A > C polymorphism might modify Gastric cardiac adenocarcinoma susceptibility PMID: 24696261
The proportion of IL-15Ralpha expression on total leukocytes was much lower for all rheumatic diseases, including Behcet disease, than in healthy controls PMID: 23417200
Single nucleotide polymorphism in IL15RA gene is associated with ER-positive breast cancers only in American women of African ancestry. PMID: 23996684
lower frequencies of IL-15RA-positive T cells in Behcet's disease PMID: 23618691
Epidermal IL-15Ralpha acts as an endogenous antagonist of psoriasiform inflammation in mouse and man. PMID: 24019554
The inflammatory bowel diseases patients have an increased expression of IL-15Ralpha mRNA in the mucosa; expression is localized in B cells, suggesting that IL-15 regulates B-cell functions during bowel inflammation. PMID: 23039249
The expression of IL-15Ralpha on CD8 T cells is required for uncontrolled aggressive lymphoproliferation; none of the IL-15Ralpha(-/-)-IL-15 mice that we followed for more than 2 years developed the fatal disease despite controlled expansion of CD8 T cells PMID: 21304101
IL-15 is produced and secreted only as a heterodimer with IL-15Ralpha. PMID: 22496150
High serum IL-15R alpha is associated with T-cell large granular lymphocyte leukemia. PMID: 22049515
These results suggest that IL15RA polymorphism may be associated with the susceptibility of ossification of the posterior longitudinal ligament in Korean population. PMID: 21689944
Different levels of IL-15 trans-presentation are required for different natural killer (NK) cell developmental events to reach full maturation status PMID: 21715685
broad expression pattern of functional IL-15RA splicing forms and suggests a regulatory role of DNA methylation in IL-15RA transcript Var1 expression in mononuclear cells PMID: 21097393
mRNA for IL-15 receptor alpha was constitutively expressed in all tested human fetal brain structures, indicating a role in their development and physiology PMID: 12114302
interleukin-15alpha receptor binds to IL-15 at specific binding sites, one in the B helix and the other in the C helix PMID: 15039446
Soluble IL-15R alpha arises from proteolytic shedding of the membrane-anchored receptor. It is an inhibitor of IL-15 binding to the membrane receptor & of IL-15-induced cell proliferation. IL-15R alpha shedding may have major immunoregulatory functions. PMID: 15265897
IL-15 is an important mediator of muscle mass response to resistance exercise training in humans and that genetic variation in IL15RA accounts for a significant proportion of the variability in this response. PMID: 15531573
Study of three-dimensional structure of IL-15 receptor (IL-15R) alpha chain has led to a model of the IL-15.IL-15R alpha complex that reveals involvement of a large network of ionic interactions not observed in other cytokine/cytokine receptor complexes. PMID: 16377614
Results show that the biological activity of soluble IL-15 is much improved after interaction with recombinant soluble IL-15Ralpha. PMID: 16757567
Data show that NK cell survival mediated through the regulatory synapse with human dendritic cells requires IL-15Ralpha. PMID: 17948125
sIL-15Ralpha has a protumor role in cancer PMID: 18483276
genetic variability of the IL-15 receptor has an important role in body fat composition. PMID: 19309557
IL-15 receptor alpha facilitates the stability and secretion of the IL-15 short signal peptide, a soluble and bioactive isoform. PMID: 19696432

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.