Recombinant Human Interleukin-27 Subunit Beta (EBI3) Protein (His-GST)

Name: Recombinant Human Interleukin-27 Subunit Beta (EBI3) Protein (His-GST)
Brand: Beta LifeScience
SKU: BLC-01663P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Human Interleukin-27 Subunit Beta (EBI3) Protein (His-GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q14213
Target Symbol	EBI3
Synonyms	IL-27 subunit beta;IL-27B;Epstein-Barr virus-induced gene 3 protein homolog
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-GST
Target Protein Sequence	RKGPPAALTLPRVQCRASRYPIAVDCSWTLPPAPNSTSPVSFIATYRLGMAARGHSWPCLQQTPTSTSCTITDVQLFSMAPYVLNVTAVHPWGSSSSFVPFITEHIIKPDPPEGVRLSPLAERQLQVQWEPPGSWPFPEIFSLKYWIRYKRQGAARFHRVGPIEATSFILRAVRPRARYYVQVAAQDLTDYGELSDWSLPATATMSL
Expression Range	21-227aa
Protein Length	Partial
Mol. Weight	54.6 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	Associates with IL27 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells, and that has diverse effects on innate immune cells. Among its target cells are CD4 T-helper cells which can differentiate in type 1 effector cells (TH1), type 2 effector cells (TH2) and IL17 producing helper T-cells (TH17). It drives rapid clonal expansion of naive but not memory CD4 T-cells. It also strongly synergizes with IL-12 to trigger interferon-gamma/IFN-gamma production of naive CD4 T-cells, binds to the cytokine receptor WSX-1/TCCR. Another important role of IL-27 is its antitumor activity as well as its antiangiogenic activity with activation of production of antiangiogenic chemokines.
Subcellular Location	Secreted.
Protein Families	Type I cytokine receptor family, Type 3 subfamily
Database References	HGNC: 3129 OMIM: 605816 KEGG: hsa:10148 STRING: 9606.ENSP00000221847 UniGene: Hs.501452

Gene Functions References

The IL-35 levels in CagA(+) H. pylori-infected participants from peptic ulcer and H. pylori-infected asymptomatic groups were lower than individuals infected with CagA(-) strains. PMID: 29938865
IL-35 may be involved in the pathogenesis of Primary biliary cirrhosis. PMID: 29445068
IL-35 is a relatively newly discovered member of the IL-12 family which are unique in structure as they are dimer formed by two subunits; recent findings have shown abnormal expression of IL-35 in inflammatory autoimmune diseases and functional analysis suggested that IL-35 is critical in the onset and development of these diseases. [Review] PMID: 29729445
IL-35 expression was significantly increased in patients with chronic hepatitis C and was positively correlated with the levels of viral RNA PMID: 28644966
Pancreatic ductal carcinoma cells produce IL35 to recruit monocytes via CCL5 and induce macrophage to promote angiogenesis via expression of CXCL1 and CXCL8. PMID: 28989066
The study revealed that post-therapeutic recovery of circulating IL-35 concentration might be an independent predictor for effective response to IST in pediatric AA. PMID: 28211781
The plasma levels of interleukin-35 were significantly higher in the hepatocellular carcinoma patients than the controls. PMID: 27699510
this study introduces IL-35 as a new treatment for pemphigus PMID: 27855302
over-expression of EBI3 could reduce the apoptosis of Treg/CD4(+)T/CD8(+)T cells and prevent radiation-induced immunosuppression of cervical cancer HeLa cells by inhibiting the activation of PD-1/PD-L1 signaling pathway PMID: 28351328
Data show that interleukin-35 (Epstein-Barr virus-induced gene 3 (EBI3) and the interleukin-12 Subunit p35 (p35) subunit) levels were significantly elevated in the patients with influenza infection. PMID: 26844658
higher decidual mRNA expression in preeclampsia PMID: 26472010
IL-35 was elevated in bone marrow of adult AML patients and this increase was correlated with the clinical stages of malignancy, suggesting that IL-35 is involved in pathogenesis of AML. PMID: 26431888
Elevated circulating IL-35, particularly at early phase, its decrease after treatment initiation, and a positive association between synovial fluid IL-35 and disease activity support an involvement of IL-35 in the pathogenesis of RA. PMID: 26204444
Data suggest that the toll like receptor 3 (TLR3)-interferon regulatory factor 6 protein (IRF6)-interleukin-23 subunit p19 (p19)/EBI3 protein axis may regulate keratinocyte functions in the skin. PMID: 26303210
EBI3 gene rs4740 polymorphism is closely associated with susceptibility to pulmonary tuberculosis and the elevation and enrichment of EBI3 in the lung derived from macrophages may contribute to the exacerbation of mycobacterial infection. PMID: 25937126
EBI3 Downregulation Contributes to Type I Collagen Overexpression in Scleroderma Skin. PMID: 26355156
IL-35 mRNA and protein were higher in tuberculous pleural effusions than in malignant ones. PMID: 25935866
IL-35 can effectively suppress the proliferation and IL-4 production of activated CD4+CD25- T cells in allergic asthma, and that IL-35 may be a new immunotherapy for asthma patients. PMID: 26044961
IL-35 is highly expressed in chronic HBV CD4(+) T-cells and plays an important role in the inhibition of the cellular immune response in chronic HBV. PMID: 25869609
The levels of EBI3 and IL-12p35 mRNAs in peripheral blood mononuclear cells in moderate or hyper-responders were significantly higher than those in non- or hypo-responders. PMID: 25575066
The results suggest that the decreased expression of IL-35 could be involved in the pathogenesis of childhood asthma. PMID: 24970690
IL-17 and IL-35 may be critically involved in the pathogenesis of hepatitis B-related LC. PMID: 25323532
IL35 appears to contribute to the loss of immunological self-tolerance in ITP patients by modulating T cells and immunoregulatory cytokines. PMID: 25640666
IL-35 levels are dramatically decreased in immune thrombocytopenia patients, suggesting that IL-35 may be involved in the pathogenesis of this disease. PMID: 24994465
Interleukin-35 induces regulatory B cells that suppress autoimmune disease. [il-35] PMID: 24743305
ingestion of apoptotic cells by DCs leads to increased expression of IL-12p35 and Ebi3 without affecting IL-12p40. PMID: 24782489
circulating IL-35 in PDAC patients significantly increased, suggesting that regulating the expression of IL-35 may provide a new possible target for the treatment of PDAC patients, especially for the resectable ones. PMID: 24121041
The increased expression of IL-35 in chronic and aggressive periodontitis suggests its possible role in pathogenesis of periodontitis. PMID: 24376289
EBI3-overexpression in MRL/lpr mice induces generation of regulatory T cells, causing suppression of autoimmune and inflammatory reactions by affecting the T helper (Th)1 cell/Th2 cytokine balance. PMID: 23845089
in contrast to TGF-beta, IL-35 is not constitutively expressed in tissues but it is inducible in response to inflammatory stimuli PMID: 22438968
the findings from the past decade identify IL-27 as a critical immunoregulatory cytokine, especially for T cells, whereas some controversy is fueled by results challenging the view of IL-27 as a classical silencer of inflammation. PMID: 23904441
expressed by trophoblast cells PMID: 23619469
The findings of this study suggest that SNPs in FOXP3 and EBI3 genes modify the risk for development of chronic rhinosinusitis. PMID: 23562195
these results reveal a novel functional role for IL-35 in suppressing cancer activity, inhibiting cancer cell growth, and increasing the apoptosis sensitivity of human cancer cells through the regulation of genes related to the cell cycle and apoptosis. PMID: 23154182
The findings of this study support the potential role of regulatory T cells and genetic variations in the regions around FOXP3 and EBI3 genes in modifying the risk for AR development in Chinese patients. PMID: 22836044
This study demonstrated that interleukin-35 expression could be detected in the CD4(+) T cells from peripheral blood of chronic hepatitis B patients. PMID: 21285006
IL-27 expression is one host immune factor produced in response to influenza A virus infection and that elevated IL-27 levels inhibit viral replication. PMID: 22343630
Data show that Epstein-Barr virus-induced gene 3 (EBI3) is differentially expressed among Burkitt lymphoma and diffuse large B-cell lymphoma. PMID: 21931777
a new heterodimeric cytokine that consists of EBI3, an IL-12p40-related protein, and p28, a newly discovered IL-12p35-related polypeptide (IL-27) PMID: 12121660
results suggest that increased numbers of Epstein-Barr virus-infected cells in areas of active inflammatory bowel disease are secondary to influx or local proliferation of inflammatory cells & do not contribute significantly to local production of EBI3 PMID: 15170639
findings indicate that the restricted Th1 responses in newborns owing to deficient IL-12 production may be compensated for, in part, by enhanced IL-27 secretion PMID: 18167155
The genome-wide mRNA expression profile under the condition of short-term stimulation (4h) with IL-18 using the Affymetrix GeneChip((R)) Array System, was characterized. PMID: 18336908
Our data support a possible role of Ebi3 in atherogenesis PMID: 19556516

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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.

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