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Description: Human IL-33, also called NF-HEV and DVS 27, is a 30 kDa proinflammatory cytokine produced by endothelial and epithelial cells. IL-33 is released during necrotic cell death but was first found in the nucleus of endothelial cells. This dual pattern of expression is reminiscent of "alarmins" also known as endogeneous danger signals. Other known alarmins are IL-1 alpha and HMGB1. IL-33 has been identified as the ligand for ST2 (also known as IL-33 receptor, a member of the IL-1 receptor family). ST2 is stably expressed on mast cells and Th2 effector T cells and is functionally associated with Th2-mediated inflammation. Although IL-33 was initially reported to be processed by Caspase-1, recent data indicate that Caspase-3 or -7 are capable of processing IL-33 at more physiologic concentrations. IL-33 plays an immune regulatory role by inducing IL-5 and IL-13 in vitro and in vivo and activating basophils, eosinophils and mast cells. In addition to its role in proinflammation, it may also decrease inflammation through interactions with IL-1 thereby blocking its effect. Human IL-33 shares 55% amino acid sequence identity with mouse.
Applications Reported: Human IL-33 Recombinant Protein Carrier-Free is biologically active and can promote the proliferation of D10S cells in culture.
Applications Tested: The ED50 of this protein, as measured by proliferation of mouse D10S cells, is less than or equal to 0.05 ng/mL.
Source: E. coli-expressed amino acids Ser112 -Thr270 (Accession #NM_033439).
Bioactivity: The ED50 of this protein, as measured by proliferation of mouse D10S cells, is less than or equal to 0.05 ng/mL.
Endotoxin: Less than 0.1 ng/ug cytokine as determined by the LAL assay. Purity: >98% as determined by SDS-PAGE and HPLC.
Molecular Weight: 21 kDa.
Storage and handling: Use in a sterile environment. Store lyophilized protein at less than or equal to -20°C. Reconstituted protein solution can be stored with carrier protein (e.g., 0.1% BSA) at less than or equal to -20°C.
IL-33 (Interleukin-33) is a 270 amino acid, highly divergent protein belonging to the IL-1 family with an IL-1-like C-terminal domain. IL-33 is a dual function protein that may function both as a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties. IL-33 binds to and signals through IL1RL1/ST2 and its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6. IL-33 activates NF-kappaB and MAP kinases, and drives production of TH2-associated cytokines from in vitro polarized TH2 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. IL-33 is proteolytically converted to a mature form by CASP1 and is highly expressed in high endothelial venules found in tonsils, Peyer's patches and mesenteric lymph nodes and is almost undetectable in placenta. Prolonged IL-33 treatment of mice led to the development of eosinophilia, splenomegaly, and severe pathological changes in mucosal organs such as lungs, esophagus and small intestine. Recent experiments have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine and an intracellular nuclear factor with transcriptional regulatory properties. Despite its predicted molecular weight, IL-33 will often run at higher molecular weight in SDS-PAGE. Studies have shown that IL-33 can also co-localize with heterochromatin and possesses transcriptional repressor activities, indicating that IL-33 may function as both a proinflammatory cytokine, and an intracellular nuclear factor with transcriptional regulatory properties.
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