Recombinant Human IL36G Protein

Name: Recombinant Human IL36G Protein
Brand: Beta LifeScience
SKU: BL-1676SG
Availability: InStock

Collections: Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	Q9NZH8
Synonym	IL1RP2, IL-1 epsilon, IL1F9, IL1H1
Background	Human IL36G is a secreted member of the IL1 family, one of three IL36 genes in humans. The IL1 family members display a conserved 12 b-strand and a b-trefoil configuration, likely due to ascendance from a mutual ancenstral gene. IL36G is expressed primarily in tissues containing epithelial cells, and is both intracellular and secreted. Its primary receptor appears to be a combination of IL-1rp2 and IL-1Racp, the first being primarily expressed on dendritic cells and the second being more widely expressed. Binding of IL36G ligands to this receptor is one of the factors which induces dendritic cell maturation. Its expression is also an agonist for pro-inflammatory cytokines through the NF-kB and Map kinase pathways. Recombinant human IL36G migrates as an 18.9 kDa protein on SDS-PAGE and shares approximately 52% sequence identity with mouse IL36G.
Description	Recombinant Human IL36G was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	18.9 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human IL36G Protein should be stored should be stored at < -70°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. 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; also stimulates its own expression and that of the prototypic cutaneous proinflammatory parameters TNF-alpha, S100A7/psoriasin and inducible NOS. May play a role in proinflammatory responses during particular neutrophilic airway inflammation: activates mitogen-activated protein kinases and NF-kappa B in primary lung fibroblasts, and stimulates the expression of IL-8 and CXCL3 and Th17 chemokine CCL20 in lung fibroblasts. May be involved in the innate immune response to fungal pathogens, such as Aspergillus fumigatus.
Subcellular Location	Cytoplasm. Secreted.
Protein Families	IL-1 family
Database References	HGNC: 15741 OMIM: 605542 KEGG: hsa:56300 STRING: 9606.ENSP00000259205 UniGene: Hs.211238
Tissue Specificity	Highly expressed in tissues containing epithelial cells: skin, lung, stomach and esophagus. Expressed in bronchial epithelial. In skin is expressed only in keratinocytes but not in fibroblasts, endothelial cells or melanocytes. Up-regulated in lesional ps

Gene Functions References

serum IL-36gamma levels were higher in active systemic lupus erythematosus patients and correlated with disease activity and arthritis PMID: 29571080
Cathepsin S was identified as the major IL-36gamma-activating protease expressed in epithelial cells. PMID: 28289191
enhanced expression of IL-36gamma was observed in plasma and bronchoalveolar lavage fluid of patients with acute respiratory distress syndrome because of bacterial pneumonia PMID: 28176791
IL-36-mediated IL-6 and CXCL8 production in human lung fibroblasts and bronchial epithelial cells may be involved in pulmonary inflammation especially caused by bacterial or viral infections. PMID: 28869889
With a focus on the skin as a target for microbial and viral invasion, the current knowledge of IL-36: IL-36alpha, IL-36beta and IL-36gamma, functions is reviewed. One physiological function of the IL-36smay be to counteract microbial immune evasion. [Review] PMID: 28811383
IL-36gamma inhibits differentiation and induces inflammation of keratinocyte via Wnt signaling pathway in psoriasis. PMID: 28924372
IL-36gamma-stimulated endothelial cells secrete the proinflammatory chemokines IL-8, CCL2 and CCL20. PMID: 27673278
skin injury increases IL-36gamma via the activation of TLR3-SLUG-VDR axis and IL-36gamma induces REG3A to promote wound healing PMID: 28774595
Autocrine and Paracrine Regulation of Keratinocyte Proliferation through a Novel Nrf2-IL-36gamma Pathway PMID: 27183581
Here the authors show that Mycobacterium tuberculosis infection of macrophages induces IL-36gamma production in a 2-stage-regulated fashion. PMID: 27389350
IL-36gamma, a member of the IL-1 superfamily, is involved in host defense and contributes to proinflammatory responses and development of inflammatory diseases. PMID: 27853811
IL-36gamma is significantly more strongly expressed in the epidermis of patients with psoriasis-based erythroderma than in other inflammatory skin diseases. PMID: 26524325
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
IRF6 is likely to promote inflammation to P. gingivalis through its regulation of IL-36gamma. PMID: 26819203
Findings indicate that Interleukin (IL)-1beta-induced interleukin 36 gamma (IL-36gamma) expression is mediated by the activation of transcriptional factors, NF-kappaB p65 and AP-1 (c-jun). PMID: 26562662
IL36G was identified as strong regulators of skin pathology in both lesional and non-lesional skin samples. PMID: 25897967
Decreased Langerhans cell responses to IL36G: altered innate immunity in patients with recurrent respiratory papillomatosis PMID: 24950037
IL-36gamma expression inversely correlated with the progression of human melanoma and lung cancer. PMID: 26321222
IL-36gamma is a valuable biomarker in psoriasis patients, both for diagnostic purposes and measurement of disease activity during the clinical course PMID: 25525775
CAMP induces IL-36gamma expression leading to initiation of skin inflammation and occasional exacerbations of psoriasis. PMID: 25305315
IL-36 promotes myeloid cell infiltration, activation, and inflammatory activity in skin PMID: 24829417
This is the first report of extracellular release of endogenous IL-36gamma through pyroptosis suggesting a function of IL-36gamma as an alarmin. PMID: 22318382
Data presented herein shed further light on involvement of T-bet in innate immunity and suggest that IL-36gamma, besides IFNgamma, may contribute to functions of this transcription factor in immunopathology. PMID: 23095752
Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36alpha, IL-36beta, and IL-36gamma) or antagonist (IL-36Ra) activity PMID: 21965679
Regulation and function of the IL-1 family cytokine IL-1F9 in human bronchial epithelial cells. PMID: 20870894
Expression of IL-1F9 is increased in human plaque psoriasis skin and is overexpressed in a transgenic mouse psoriasis model. PMID: 21242515
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 PMID: 14734551
This is the first report of IL-1 genotype association with the inflammation of skeletal muscle following acute resistance exercise that may potentially affect the adaptations to chronic resistance exercise. PMID: 15331687
This report demonstrates expression of IL1F9 by bronchial epithelial cells induced by pro-inflammatory stimuli, suggesting a function of this molecule in airway inflammation. PMID: 15701729

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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.