Recombinant Human IL-33 Protein

Name: Recombinant Human IL-33 Protein
Brand: Beta LifeScience
SKU: BL-1796NP
Availability: InStock

BL-1796NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Interleukin-33 is produced by our E.coli expression system and the target gene encoding Ser112-Thr270 is expressed.
Accession	O95760
Synonym	Interleukin-33; IL-33; Interleukin-1 Family Member 11; IL-1F11; Nuclear Factor From High Endothelial Venules; NF-HEV; IL33; C9orf26; IL1F11; NFHEV
Gene Background	Interleukin-33 (IL-33) was initially discovered as a nuclear factor NF-HEV abundantly expressed in high endothelial venules. It is a 30-32 kD pro-inflammatory protein with intracellular and extracellular activities and a chromatin-associated cytokine of the IL-1 family with high sequence and structural similarity to IL-1 and IL-18. IL-33 is highly and selectively expressed by high endothelial venule endothelial cells (HEVECs) in human tonsils, Peyers's patches, and lymph nodes. It contains a bipartite nuclear localization signal at the C-terminus, and is targeted to the nucleus when ectopically expressed in human umbilical vein endothelial cells (HUVECs) and HeLa cells. The C-terminal fragment, corresponding to mature IL-33, binds and triggers signaling. IL-33 mediates its biological effects via Toll-interleukin 1 (IL-1) receptor (TIR) domain-containing receptor ST2, activates NF-kappaB and MAP kinases, and drives production of T(H)2-associated cytokines from in vitro polarized T(H)2 cells. In vivo, IL-33 induces the expression of IL-4, IL-5, and IL-13 and leads to severe pathological changes in mucosal organs. Human IL-33 is 270 amino acids in length.
Molecular Mass	18.1 KDa
Apmol Mass	18 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Endotoxin	Less than 0.001 ng/µg (0.01 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Biologically active. Please contact us to obtain bioactivity data.
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 that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells. Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines. Also involved in activation of mast cells, basophils, eosinophils and natural killer cells. Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury.; In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets. This form is rapidely lost upon angiogenic or proinflammatory activation.
Subcellular Location	Nucleus. Chromosome. Cytoplasm. Cytoplasmic vesicle, secretory vesicle. Secreted.
Protein Families	IL-1 family
Database References	HGNC: 16028 OMIM: 608678 KEGG: hsa:90865 STRING: 9606.ENSP00000370842 UniGene: Hs.731660
Tissue Specificity	Expressed at high level in high endothelial venules found in tonsils, Peyer patches and mesenteric lymph nodes. Almost undetectable in placenta.

Gene Functions References

IL-33 has a role in the pathogenesis of autoimmune hepatitis (AIH) and affects the expression of IL-4, IL-17A, and of hypergammaglobulinemia PMID: 30034292
The serum levels of IL-33 and IL-31 were significantly up-regulated in both AR and allergic asthma patients compared with normal individuals. PMID: 30301503
chromatin binding is a post-translational mechanism that regulates the releasability and ST2-mediated bioactivity of IL-33. PMID: 30108214
Results indicate that the interaction between FLIL33 and IPO5 is localized to a specific segment of the FLIL33 protein, is not required for nuclear localization of FLIL33, and protects FLIL33 from proteasome-dependent degradation. PMID: 29127199
Data suggest that targeting interleukin 33 (IL-33) may be an effective treatment for sepsis-induced immunosuppression. PMID: 28374774
Oxidative stress is involved in the expression of IL-33 in airway epithelial cells via MAPK signal pathway and IL-33 expression is augmented during viral infection. PMID: 29587772
IL-33 expression plays an important role in patients with chronic rhinosinusitis with nasal polyp. PMID: 29186722
IL-33(high) cholangiocarcinomas may represent a unique, less aggressive carcinogenetic process of the large bile ducts PMID: 29675965
Our data suggest that IL-33 produced by M2 macrophages might contribute to the pathogenesis of IgG4-RD via aberrant activation of Th2 immune responses. PMID: 28205524
The GLDC/IL33 locus on chromosome 9p24.1 as associated with overall survival in patients with osteosarcoma. PMID: 29210060
Serum and sputum IL-33 levels were higher in chronic obstructive pulmonary disease subjects with sputum eosinophilia compared to those with a normal eosinophil count. PMID: 29859068
Studies suggest that IL-33 acts as a possible pathogenic role in allergic diseases mainly by instructing the activation of various ST2-expressing cells and the production of several immune factors. The mechanisms underlying IL-33-mediated inflammation have been immunologically analyzed. However, much remains regarding the accurate functions and underlying mechanisms of the IL-33-ST2 signaling pathway. [review] PMID: 29987222
Higher IL-33 and lower s-ST2 receptor baseline serum levels were detected in Pru p 3--sensitized allergic patients (SAP). IL-33/s-ST2 ratio is increased in Pru p 3-SAP and more in patients who experienced severe systemic symptoms. PMID: 29774370
Strong immune reaction to herpes virus infection may depend on strong IL-33 expression in the epidermis, while very weak immune reaction in samples from patients with verruca vulgaris may be due to low or no expression of IL-33 in the lesional epidermis. PMID: 29696682
data indicate that during acute, resolving colitis, IL-33/ST2 plays a crucial role in gut mucosal healing by inducing epithelial-derived miR-320 that promotes epithelial repair/restitution and the resolution of inflammation. PMID: 30224451
IL-33 facilitates proliferation of colorectal cancer dependent on COX2/PGE2. IL-33 functions via its receptor ST2 and upregulates COX2 expression through NF-kappaB signaling. Understanding the IL-33 signal transduction in colorectal cancer (CRC)cells provides potential therapeutic targets for clinical treatment PMID: 30119635
Preincubation of LAD2 cells with the natural flavonoid methoxyluteolin (1-100 mM) inhibits (P < 0.0001) secretion and gene expression of IL-1beta, procaspase-1, and pro-IL-1beta. Mast cell secretion of IL-1beta in response to SP and IL-33 reveals targets for the development of antiinflammatory therapies. PMID: 30232261
IL-33 could be suggested as a novel biomarker to distinguish different types of Salivary gland tumors PMID: 29991126
IL-33 can regulate deposition of ECM and promote the process of pulmonary fibrosis by inducing the imbalance between MMP-9 and TIMP-1. PMID: 29417309
these data demonstrate the expression of IL33 in oral lichen planus lesions PMID: 29633015
The aim of this study was to explore the possible correlations of serum interleukins and soluble ST2 (sST2) protein with clinical features and inflammatory cytokines in rheumatoid arthritis (RA) patients. PMID: 29798971
IL-33 may down-regulate CLDN1 expression through the ERK/STAT3 pathway in keratinocytes. PMID: 29534857
IL-33 promotes Renal Cell Carcinoma cell proliferation and chemotherapy resistance via its receptor ST2 and the JNK signaling activation in tumor cells. PMID: 29763892
Low IL-33 expression is associated with experimental autoimmune encephalomyelitis susceptibility only in females. PMID: 29378942
High IL33 expression is associated with schistosome infection. PMID: 29554131
Serum IL-33 levels were significantly higher in patients with Behcet's disease compared to the healthy controls. PMID: 28412856
In the present review, we have discussed the cellular sources, modes of action and regulation of IL-17 and IL-33 in the context of hypersensitive diseases [Review] PMID: 29153708
results suggest that IL-33 acts as a cytokine but not as a nuclear factor regulating gene expression in endothelial cells PMID: 27694941
IL-33 increased IL-10 expression in MFCs via activating ERK 1/2 and STAT3, which subsequently promoted IL-10 transcription and thus contributed to the beneficial effects of IL-33 on MFCs. PMID: 29099095
IL-33 contributes to hepatic granuloma pathology through induction of M2 macrophages during S. japonicum infection. PMID: 27445267
Serum levels of ST2, IL-33 and BNP were independent risk factors for major adverse cardiovascular events in acute myocardial infarction after percutaneous coronary intervention. PMID: 28623858
Recombinant human IL33 inhibited trophoblast invasion and adhesion, and decreased adhesion and invasionassociated molecules such as integrin alpha4beta1 and CD62L. PMID: 28765940
TNF synthesis and secretion by mast cells is amplified by interactions of substance P and IL-33. PMID: 28461492
Interleukin-33 signaling contributes to renal fibrosis following ischemia reperfusion PMID: 28668506
Findings indicate that IL33 may be involved in the process of glioma cell invasion and migration by upregulating MMP2 and MMP9 via the ST2-NF-kappaB signaling pathway. PMID: 28849217
IL-33 deficiency in mice does not lessen liver fibrosis during diet-induced steatohepatitis, in contrast to previous studies indicating a deleterious role of exogenous IL-33 in chronic liver injury and experimental NAFLD. PMID: 28611297
The downregulation of epithelial IL-33 expression may potentially serve as a marker for disease remission in UC together with other biomarkers including mucosal TNF. PMID: 27748438
Findings indicate that IL-10 act as a negative regulator of IL-33/ST2 signaling pathways in vivo. PMID: 28415811
Study identify that IL-33 expression is reduced in many carcinomas upon their transition to the metastatic form of disease and, appears to be directly correlated with MHC-I and possibly co-regulated. These results suggest that the down-regulation of IL-33 takes place concomitantly with the transition from primary to metastatic tumors and represents an entirely new form of tumor immune-escape. PMID: 27619158
The proinflammatory cytokine IL-33 induces differential tissue factor expression and activity in monocyte subsets, as well as the release of procoagulant microvesicless. In this manner, IL-33 may contribute to the formation of a prothrombotic state characteristic for cardiovascular disease. PMID: 28492698
this review and meta-analysis showed that serum IL33 is a helpful biomarker for early diagnosis of childhood asthma PMID: 28410870
IL-33 down-regulates the induction of hCAP-18/LL-37 production in human gingival epithelial cells. PMID: 28637951
We found significantly higher serum IL-33 and soluble ST2 levels in patients with active adult-onset Still's disease. Results indicate that the IL-33/ST2 signaling pathway may play a role in the pathogenesis of the acute inflammation and skin manifestations associated with adult-onset Still's disease. PMID: 28365573
IL-33 expression is associated with age and invasive depth of GC patients. PMID: 28000059
serum levels elevated in both idiopathic granulomatous mastitis and breast cancer PMID: 27780363
IL-33 induces IL-8 expression via JNK/c-Jun/AP-1 pathway in human vascular endothelial cells, and provides a new insight into the role of IL-33-induced IL-8 in the pathophysiology of atherosclerosis and vascular inflammation PMID: 29373608
a relationship between glucose homeostasis and the IL-33/ST2 axis after transplantation PMID: 28013014
The results of the present study indicate that ISTP may inhibit TARC/CCL17 production in human epidermal keratinocytes via the STAT1 signaling pathway and may be associated with the inhibition of IL33 production. PMID: 28447741
Data suggest that interleukin-33 (IL-33) isoforms activate basophils and mast cells to drive type 2 inflammation in chronic stable asthma. PMID: 27432971
Through induction of TF in vascular endothelial cells, IL-33 could enhance their thrombotic capacity and thereby might impact on thrombus formation in the setting of atherosclerosis. PMID: 27142573

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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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