Recombinant Human IL1F6 Protein (aa 6-158)

Beta LifeScience SKU/CAT #: BLPSN-2771

Recombinant Human IL1F6 Protein (aa 6-158)

Beta LifeScience SKU/CAT #: BLPSN-2771
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Product Overview

Tag aa 6-158
Host Species Human
Accession Q9UHA7
Synonym 1E, FIL, FIL1, FIL1(EPSILON), FIL1E, IL-1F6, IL1(EPSILON), IL1E, IL1F6, IL36A
Background Interleukin-1 family member 6 (IL-1F6), also known as interleukin 36, alpha (IL36A), is a pro-inflammatory cytokine which plays an important role in innate and adaptive immunity. IL-1F6 activates MAPK and NF-kB pathways and is produced by many different cells. This cytokine is a family member of interleukin-1 (IL-1) and plays an important role in the pathophysiology of several diseases. It has been reported that IL-1F6 and IL-1F8, in addition to IL-1F9, activate the pathway leading to NF-kappaB in an IL-1Rrp2-dependent manner in Jurkat cells as well as in multiple other human and mouse cell lines. Activation of the pathway leading to NF-kappaB by IL-1F6 and IL-1F8 follows a similar time course to activation by IL-1beta, suggesting that signaling by the novel family members occurs through a direct mechanism. In a mammary epithelial cell line, NCI/ADR-RES, which naturally expresses IL-1Rrp2, all three cytokines signal without further receptor transfection. IL-1Rrp2 antibodies block activation of the pathway leading to NF-kappaB by IL-1F6, IL-1F8, and IL-1F9 in both Jurkat and NCI/ADR-RES cells. Thus IL-1F6, IL-1F8, and IL-1F9 signal through IL-1Rrp2 and IL-1RAcP.
Description A DNA sequence encoding the human IL1F6 (Q9UHA7) (Ala6-Phe158) was expressed and purified, with two additional amino acids (Gly & Pro) at the N-terminus.
Source E.coli
Predicted N Terminal Gly
AA Sequence Ala6-Phe158
Molecular Weight The recombinant human IL1F6 consists of 155 a.a. and predicts a molecular mass of 17 .2 KDa. It migrates as an approximately 18 KDa band in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Measured by its ability to induce IL8 secretion in A431 human epithelial carcinoma cells. The ED50 for this effect is typically 5-20 ng/mL.
Formulation Lyophilized from sterile PBS pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of proinflammatory cytokines such as TNF-alpha, IL-8 and IL-6. In cultured monocytes upregulates expression of IL-1A, IL-1B and IL-6. In myeloid dendritic cells involved in cell maturation by upregulating surface expression of CD83, CD86 and HLA-DR. In monocyte-derived dendritic cells facilitates dendritic cell maturation and drives T-cell proliferation. May play a role in proinflammatory effects in the lung.
Subcellular Location Cytoplasm. Secreted.
Protein Families IL-1 family
Database References
Tissue Specificity Expressed in immune system and fetal brain, but not in other tissues tested or in multiple hematopoietic cell lines. Predominantly expressed in skin keratinocytes but not in fibroblasts, endothelial cells or melanocytes. Increased in lesional psoriasis sk

Gene Functions References

  1. serum IL-36alpha levels were higher in active systemic lupus erythematosus patients and correlated with disease activity and arthritis PMID: 29571080
  2. Data suggest that interleukin-36alpha (IL-36alpha) plays an important role in the pathophysiology of inflammation and fibrosis in the pancreas via an autocrine function. PMID: 28099250
  3. The data identify a novel role for IL-36 signaling in colonic inflammation and indicate that the IL-36R pathway may represent a novel target for therapeutic intervention. PMID: 26813344
  4. IL-36a was displayed to be able to suppress the growth of epithelial ovarian cancer cells in our setting, which is suggestive of its druggable potential in curing the epithelial ovarian cancer and that upregulation of IL-36a was found to be capable of inhibiting the growth of epithelial ovarian cancer cells. PMID: 28621240
  5. Increased Expression of Interleukin-36 is associated with Inflammatory Bowel Disease. PMID: 26752465
  6. IL-36alpha acts as a pro-inflammatory cytokine at cartilage level, by increasing the expression of markers of inflammation and cartilage catabolism. PMID: 26560022
  7. Study shows that plasma concentrations of IL-36alpha and IL-36gamma are overexpressed in active systemic lupus erythematosus patients and that IL-36alpha has a substantial pro-inflammatory effect through regulation of IL-6 and CXCL8 production. PMID: 26516833
  8. increases maturation of monocyte-derived dendritic cells PMID: 25700962
  9. IL36A-IL36R axis is modulated in patients with primary Sjogren's syndrome. PMID: 25902739
  10. IL-36alpha was highly expressed in nearly half of all colorectal cancer patients. Low expression level of IL-36alpha correlated with larger tumor size and advanced cancer stage. Low expression of IL-36alpha resulted in a poor prognosis of colorectal cancer patients. PMID: 25550854
  11. Results show that IL-36alpha expression may play a pivotal role in determining the prognosis of hepatocellular carcinoma (HCC). PMID: 24061617
  12. The novel cytokine interleukin-36alpha is expressed in psoriatic and rheumatoid arthritis synovium. PMID: 23268368
  13. Expression of IL-1F6 is increased in human plaque psoriasis skin and in the lesional skin of transgenic mice compared with monotransgenic littermates. PMID: 21242515
  14. A functional IL-6 polymorphism has been weakly associated with level of peak bone mineral density and the rate of forearm trabecular postmenopausal bone loss in a cohort of women. PMID: 12110411
  15. Dysregulated expression in transgenic mice can promote cutaneous inflammation, revealing potential novel targets for the treatment of inflammatory skin disorders. PMID: 17908936
  16. IL-1 epsilon, an interleukin-1 agonist, activates NF-kappa B through the orphan IL-1 receptor-related protein 2 and may constitute part of an independent signaling system present in human epithelial barriers. PMID: 11466363

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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