Recombinant Human Interleukin-33/IL-33

Cat.No.: C091

Recombinant Human IL-33
Description
Recombinant Human Interleukin-33 is produced by our E.coli expression system and the target gene encoding Ser112-Thr270 is expressed.
Accession #:O95760
Known as:Interleukin-33; IL-33; Interleukin-1 Family Member 11; IL-1F11; Nuclear Factor From High Endothelial Venules; NF-HEV; IL33; C9orf26; IL1F11; NFHEV
Formulation
Lyophilized from a 0.2 μm filtered solution of 20mM PB ,150mM NaCl,pH7.4 .
Quality Control
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin:Less than 0.1 ng/?g (1 EU/?g) as determined by LAL test.
Reconstitution
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to
Storage
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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.
Publication
COMPOSITIONS AND METHODS FOR TREATING CLOSTRIDIUM DIFFICILE INFECTION Frisbee Alyse Longtin, et al. (University of Virginia Patent Foundation patent:US20190290732 2019)+
Clostridium difficile infection is the leading cause of hospital acquired antibiotic-associated diarrhea in the US (Bartlett, in 2006). The increased prevalence of circulating C. difficile strains poses a significant health threat to US health care facilities. Strains expressing the toxin C. difficile Transferase (CDT), in addition to Toxins A and B (TcdA and TcdB), are more virulent and are associated with higher mortality rates (Bacci et al., 2011). We recently identified a protective role for eosinophils against C. difficile pathogenesis (Buonomo et al., 2016). We have also defined CDT's ability to increase host inflammation and suppress protective eosinophils through a TLR2 dependent mechanism (Cowardin et al., 2016). How CDT promotes virulence and eosinophil suppression via TLR2 is still under investigation. We employed a genome-wide microarray approach to reveal divergent transcriptional profiles between protected (TLR2?/?) and unprotected (WT) mice infected with either CDT expressing or CDT mutant strains of C. difficile. This work revealed novel host mediated TLR2-dependent inflammatory pathways to CDT. We provide an unbiased framework for understanding the host immune response to the binary toxin CDT produced by C. difficile and how TLR2 signaling enhances virulence.

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