Biotinylated Recombinant Human Interleukin-26 (IL26) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-07426P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Biotinylated Recombinant Human Interleukin-26 (IL26) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-07426P
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Product Overview

Description Biotinylated Recombinant Human Interleukin-26 (IL26) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb Q9NPH9
Target Symbol IL26
Species Homo sapiens (Human)
Expression System E.coli
Tag N-MBP&C-6His-Avi
Target Protein Sequence KHKQSSFTKSCYPRGTLSQAVDALYIKAAWLKATIPEDRIKNIRLLKKKTKKQFMKNCQFQEQLLSFFMEDVFGQLQLQGCKKIRFVEDFHSLRQKLSHCISCASSAREMKSITRMKRIFYRIGNKGIYKAISELDILLSWIKKLLESSQ
Expression Range 22-171aa
Protein Length Full Length of Mature Protein
Mol. Weight 65.3 kDa
Research Area Immunology
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 May play a role in local mechanisms of mucosal immunity and seems to have a proinflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin.
Subcellular Location Secreted.
Protein Families IL-10 family
Database References
Tissue Specificity Expressed in HVS transformed T-cells but not other T-cell lines or primary stimulated T-cells. Expressed in colonic T-cells including Th17 inflammatory T-cells; the expression is significantly increased in serum of patients with Crohn's disease (at protei

Gene Functions References

  1. this paper shows that IL-26 is overexpressed in Behcet's disease and enhances Th17 related -cytokines PMID: 28811236
  2. The varIL26 genotype is associated with reduced PMN capacity to kill bacteria. A varIL26 genotype is associated with decreased levels of anti-TNF-alpha in CD patients. IL26 may help explain the role of bactDNA as a risk factor of flare in CD patients. PMID: 28879509
  3. IL-26 activates STAT1/3 and leads to the induction of IL-6 and IL-8 expression in non-transformed cells derived from human colon. PMID: 28852311
  4. IL-26 levels are higher in synovial fluid compared to plasma in spondyloarthritis. IL-26 was identified in axial facet joints of spondyloarthritis patients. Myofibroblasts from the spondyloarthritis synovium produce large amounts of IL-26. IL-26 induces bone mineralization in human osteoblasts. PMID: 28365787
  5. this study shows that IL-26 is a unique cationic protein more similar to a soluble pattern recognition receptor than to conventional cytokines PMID: 28356384
  6. this study shows that single nucleotide polymorphism near IL-26 gene is associated with familial vitiligo and existence of halo nevi in Estonian patients PMID: 26429320
  7. Our study indicates that IL-26 is a potential biomarker of disease severity in pediatric asthma without signs of Th2-mediated inflammation. PMID: 27029915
  8. IL-26 is emerging as a potentially important player in host defense and may also be a pathogenic factor in the chronic inflammatory disorders of humans. [Review] PMID: 26202572
  9. The negative influence of IL-26 on the anti-mycobacterial activity and its constitutive presence in both serum and monocyte supernatants prompt a proposal that IL26 as a candidate gene for tuberculosis susceptibility. PMID: 25157980
  10. IL-26 differentially modulates the infection by different enveloped viruses. PMID: 23875025
  11. Elevated levels of IL-26 in human gastric cancer promote proliferation and survival by modulating STAT1/STAT3 signaling. PMID: 23704922
  12. IL-26 appears as a novel proinflammatory cytokine, located upstream of the proinflammatory cascade, that may constitute a promising target to treat rheumatoid arthritis and chronic inflammatory disorders. PMID: 23055831
  13. Identify a second enhancer element positioned between IL26 and IFNG required for both IL26 and IFNG expression. One function of this enhancer is to facilitate recruitment of RNA polymerase II to promoters of both genes. PMID: 22622197
  14. common polymorphisms in the IFNgamma/IL-26 gene region may contribute to sex bias in susceptibility to rheumatoid arthritis, by distorting the propensity of female carriers versus male carriers to contract this disease. PMID: 14558082
  15. The active receptor complex for IL-26 is a heterodimer composed of two receptor proteins: IL-20 receptor 1 and IL-10 receptor 2. Signaling through the IL-26 receptor results in activation of STAT1 and STAT3. PMID: 14764663
  16. sensitivity to recombinant interleukin-26(IL-26) of various cell lines strictly correlated with the expression of IL-20 receptor 1 and blocking antibodies against either IL-10 receptor 2 or IL-20 receptor 1 inhibited IL-26-dependent signal transduction PMID: 15178681

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.

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