Biotinylated Human IL-13 Protein (C-Avi-6His)

Name: Biotinylated Human IL-13 Protein (C-Avi-6His)
Brand: Beta LifeScience
SKU: BL-2897NP
Availability: InStock

BL-2897NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Avi-tagged proteins, Cytokines, Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Interleukin-13 is produced by our Mammalian expression system and the target gene encoding Gly21Asn132 is expressed with a Avi, 6His tag at the C-terminus.
Accession	AAK53823
Synonym	Interleukin-13; IL-13
Gene Background	Interleukin-13 is also known as IL-13. It is a protein that in humans is encoded by the IL13 gene. Interleukin-13 is an immunoregulatory cytokine produced primarily by activated Th2 cells.It is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils.
Molecular Mass	15.2 KDa
Apmol Mass	22-35 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Cytokine. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses. Positively regulates IL31RA expression in macrophages.
Subcellular Location	Secreted.
Protein Families	IL-4/IL-13 family
Database References	HGNC: 5973 OMIM: 147683 KEGG: hsa:3596 STRING: 9606.ENSP00000304915 UniGene: Hs.845
Associated Diseases	Allergic rhinitis (ALRH)

Gene Functions References

forced expression of miR16 blocked NFkappaB signaling by decreasing the expression of nuclear pp65 and pIkappaBalpha, as well as increasing the expression of IkappaBalpha in IL13treated nasal epithelial cells. PMID: 30132525
These studies suggest that cellular NO excretion by the healthy epithelial mucosa is subject to considerable individual variability and may be significantly elevated among some individuals in the presence of IL-13 PMID: 29380192
This study demonstrates that IL-13 serum levels are elevated in patients with insulin resistance without showing correlation with parameters of low-grade systemic inflammation. PMID: 29675435
Our findings suggest that IL-13 SNP rs20541 is significantly associated with AR risk in Asians but not in Caucasians. [meta-analysis] PMID: 29687183
genetic variants in IL-13, especially h0011 haplotype increased the risk of the prevalence of aggregate bronchitic symptoms in non-asthmatic children. It may also modify the effects of exposure to air pollutants on the prevalence of aggregate bronchitic symptoms. PMID: 29456163
meta-analysis indicates 1112 polymorphism may be associated with susceptibility to periodontitis PMID: 29415708
These results demonstrate that histamine up-regulates the expression of TLR3 and secretion of IL-13 and MCP-1 in mast cells, thus identifying a new mechanism for the histamine inducing allergic response. PMID: 29742501
IL-13 enhances mesenchymal transition of pulmonary artery endothelial cells via down-regulation of miR-424/miR-503 in vitro. PMID: 29102771
Silencing DUOX1 by siRNA attenuated IL-13-mediated increases in superoxide, but did not reduce autophagy activities. PMID: 28982074
this is the first study using population epidemiological methods to elucidate the role of gut microbiota-related dietary factors and polymorphisms in miRNA-binding site in IL13 in CRC. PMID: 28537887
Substitutions in the central immune regulator IL13 correspond to a polymorphism linked to asthma susceptibility in humans. PMID: 28854632
IL13 polymorphism rs1295686 (in complete linkage disequilibrium with functional variant rs20541) is associated with challenge-proven food allergy. PMID: 28544327
SOCS1 inhibits epithelial IL-13 signalling, supporting its key role in regulating Th2-driven eosinophilia in severe asthma PMID: 27338192
IL-13, IL-13Ralpha1, STAT6 and ZEB1 have roles in promoting epithelial-mesenchymal transition and aggressiveness of colorectal cancer cells PMID: 27533463
This meta-analysis suggests that the T allele of rs1800925 is associated with the increased risk of COPD in both Asians and Caucasians, whereas rs20541 is associated with the risk of COPD in Caucasians but not in Asians. PMID: 29381928
the IL13-1112 C/T (rs1800925) polymorphism does not predict responsiveness to neoadjuvant chemoradiotherapy or prognosis of Chinese Han patients with locally advanced rectal cancer . PMID: 27167201
The results of this study demonstrate that IL13QD can serve as an ex vivo marker for glioma stem cells and exosomes that can inform diagnosis and prognosis of patients harboring malignant disease. PMID: 28583903
Different genotype profiles of IL13 gene seem to influence the clinical pattern of disease expression mainly confined to the upper airways, as rhinitis, or including the lower airways, as asthma PMID: 27561723
secretion of IL-13 and amphiregulin suggests Intrahepatic Innate lymphoid cells may be recruited to promote resolution and repair and thereby they may contribute to ongoing fibrogenesis in liver disease. PMID: 29261670
These findings demonstrate that NF-kappaB-mediated transcriptional mechanisms are critically involved in the IL-1beta-mediated IL-17C induction, and that IL-13 negatively regulates this induction by suppressing NF-kappaB-based transcriptional activation. PMID: 29203240
These results suggested that IL-13 +1923C/T polymorphism contributed to the development of asthma. PMID: 28057889
IL13 AA of rs20541 and STAT4 TT of rs925847 are potential genomic biomarkers for predicting lower pulmonary function. The administration of high-dose ICSs to asthmatic patients with genetic variants of IL13 AA may inhibit the advancement of airway remodelling. The genetic variants of STAT4 TT did not respond to high-dose ICSs. PMID: 26765219
The diagnostic performance of sputum IL-13 was superior to both sputum eosinophils and FeNO levels for the identification of well-controlled asthma. Sputum IL-13 levels could serve as a useful biomarker for asthma control assessment. PMID: 26990030
15LO1 inhibition (by short interfering RNA and chemical inhibitor) decreased IL-13-induced forkhead box protein A3 (FOXA3) expression and enhanced FOXA2 expression. These changes were associated with reductions in both mucin 5AC and periostin. PMID: 28723225
Clarithromycin suppressed IL-13-induced periostin production in human lung fibroblasts, in part by inhibiting STAT6 phosphorylation. This suggests a novel mechanism of the immunomodulatory effect of clarithromycin in asthmatic airway inflammation and fibrosis. PMID: 28219384
Simvastatin reversed IL-13-suppressed adenosine deaminase activity, leading to the down-regulation of adenosine signaling and inhibition osteopontin expression through the direct inhibition of IL-13-activated STAT6 pathway in COPD. PMID: 27557561
IL-13 suppressed cyp27b1 expression in CD14(+) cells. IL-13 increased expression of miR-19a in CD14(+) cells. IL-13 suppresses cyp27b1 expression in peripheral CD14(+) cells via up regulating miR-19a expression. PMID: 27381199
Leptin knockdown suppressed MUC5AC production and secretion induced by IL-13 in human bronchial epithelial cells. PMID: 28942146
demonstrate a strong association between the ratio of Acinetobacter to Proteobacteria and IL-13 production and the probability of IL-13 production after allergen exposure. IL-13 concentrations in serum were also significantly correlated with the diversity of bacterial DNA. Together, these results underscore the relationship between immune responses to allergens and bacterial exposure during perinatal development. PMID: 28443674
These observations suggest that mechanical stretch may induce an influx of Ca(2+) and up-regulation of IL-13 and MMP-9 expression in 16HBE cells via activation of TRPC1 PMID: 27986325
The presented data substantiate the hypothesis that claudin-18 is a central barrier-forming component of tight junctions and show that IL-13 downregulates claudin-18. These data also suggest that the loss of claudin-18 is associated with increased sensitization to aeroantigens and airway responsiveness PMID: 27215490
investigated the role of six potentially functional variants of the IL4, IL13, and IL4R genes in gastrointestinal cancer; both IL13 rs20541 and rs1800925 were not associated with gastrointestinal cancer risk for any of the genetic models and subgroup analyses [meta-analysis] PMID: 28142034
IL13 in bronchial epithelial cells and bronchial alveolar lavage fluid, rather than RAD50, IL4, or IL5, is more likely to be the asthma susceptibility gene. PMID: 27050946
We also found that the activation of H4R caused the release of IL-13 and RANTES on human mast cells.these data demonstrate that the H4R activates divergent signaling pathways to induce cytokine and chemokine production in human mast cells PMID: 27400655
IL13 Arg130Gln genotypes can play a role in genetic susceptibility to allergy via regulation of serum total IgE levels and affecting IFN-gamma gene expression. PMID: 28054352
The GG genotype of IL-13 130A/G cytokine gene might be involved in the induced production of total IgE and IL-13 cytokine serum levels suggesting IL-13 may be important in the signalling of asthma. PMID: 28083766
STAT6-TMEM16A-ERK1/2 signal pathway and TMEM16A channel activity are required for the IL-13-induced TMEM16A mediated mucus production PMID: 27588910
TGF-beta- and IL-13-producing mast cells might be key players in the development of bone marrow fibrosis. PMID: 28159675
this study shows that low expression of tristetraprolin is associated with glioma growth and metastasis by targeting IL-13 PMID: 27424080
this study shows that IL-13 gene polymorphism is associated with allergic rhinitis and/or allergic conjunctivitis in Finnish asthma patients PMID: 28273659
The presence of higher IL-13 and IL-17 serum levels in patients, compared with those of controls, confirms that these markers, found with high specificity, might be involved in the pathogenesis of eRA. IL-13 and IL-17 might be of better usefulness in the prediction of eRA activity status than IgM-RF and anti-CCP. PMID: 27579330
The IL13 rs20541 T allele and IL28B rs8099917 GG genotype are negative predictors of survival in patients on renal replacement therapy PMID: 26039912
these data suggest that microRNA-143 suppresses IL-13 activity and inflammation through targeting of IL-13Ralpha1 in epidermal keratinocytes PMID: 27048505
Platycodin D inhibits IL-13-induced expression of inflammatory cytokines and mucus in nasal epithelial cells by inhibiting the activation of NF-kappaB and MAPK signaling pathways. PMID: 27780139
A negative correlation between IL-13Ra2 and IL-13 was found during early infection of human schistosomiasis, suggesting an increase in cytokine in early fibrosis. PMID: 27507682
autophagy is essential for airway mucus secretion in a type 2, IL13-dependent immune disease process. PMID: 26062017
childhood asthma is associated with gene polymorphism; meta-analysis PMID: 26534891
PLD1 activation enhanced binding of ROCK1 to ATF-2 and leads to increased expression of IL-13 PMID: 26335962
DNA hypomethylation of IL13 gene may be associated with increased risk of allergic rhinitis from house dust mite sensitization PMID: 26399722
Our in vitro and in vivo data indicate close cooperation between mechanical and inflammatory stimuli on TF expression and release of TF-positive extracellular vesicles in the lungs, which may contribute to pathophysiology of asthma PMID: 26407210

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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.