Animal-Free Recombinant Human IL-1β (RMPP-00231306)
Cat. No.: RMPP-00231306
Category: Growth Factors & Cytokines
INQUIRY
2 μg
10 μg
IL-1β is a proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1α and IL-1β bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, B cell maturation and proliferation, mitogenic FGF-like activity, and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant Human IL-1β is a 17.3 kDa protein containing 153 amino acid residues.
Product Features
| Source | E.coli |
|---|---|
| Purity | ≥ 98% by SDS-PAGE gel and HPLC analyses. |
| Nature | Recombinant |
| Endotoxin Level | < 0.1 Eu/μg |
| Cross Reactivity | Frog, Human, Monkey, Mouse, Rabbit, Rat, Sheep |
Protein Information
| UniProt ID | P01584 |
|---|---|
| Molecular Weight | 17.3 kDa |
| Molecular Weight Information | M +0.61 Da (Calc. MW 17451.39 Da) |
| Sequence Similarities | Belongs to the IL-1 family. |
| Protein Length | Full length protein |
| Cellular Localization | Cytoplasm, cytosol. Lysosome. Secreted, exosome. Cytoplasmic vesicle, autophagosome. Secreted. The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. IL1B lacks any known signal sequence and the pathway(s) of its secretion is(are) not yet fully understood. On the basis of experimental results, several unconventional secretion mechanisms have been proposed. 1. Secretion via secretory lysosomes: a fraction of CASP1 and IL1B precursor may be incorporated, by a yet undefined mechanism, into secretory lysosomes that undergo Ca(2+)-dependent exocytosis with release of mature IL1B. 2. Secretory autophagy: IL1B-containing autophagosomes may fuse with endosomes or multivesicular bodies (MVBs) and then merge with the plasma membrane releasing soluble IL1B or IL1B-containing exosomes. However, autophagy impacts IL1B production at several levels and its role in secretion is still controversial. 3. Secretion via exosomes: ATP-activation of P2RX7 leads to the formation of MVBs containing exosomes with entrapped IL1B, CASP1 and other inflammasome components. These MVBs undergo exocytosis with the release of exosomes. The release of soluble IL1B occurs after the lysis of exosome membranes (By similarity). 4. Secretion by microvesicle shedding: activation of the ATP receptor P2RX7 may induce an immediate shedding of membrane-derived microvesicles containing IL1B and possibly inflammasome components. The cytokine is then released in the extracellular compartment after microvesicle lysis. 5. Release by translocation through permeabilized plasma membrane. This may occur in cells undergoing pyroptosis due to sustained activation of the inflammasome (By similarity). These mechanisms may not be not mutually exclusive. |
| Tissue Specificity | Expressed in activated monocytes/macrophages (at protein level). |
| Function | Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. |
| Post-translational Modifications | Activation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated. |
Storage & Shipping
| Shipping and Storage | Shipped on Dry Ice. |
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For research use only. Not for clinical use.
