Human IL-1 beta
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|Purity Confirmation||> 98% by SDS-PAGE|
|Molecular Weight||17.0 kDa|
|N Terminal Sequence||APVRSL and MAPVRS|
|Endotoxin Levels||< 0.1 ng per µg (IEU/µg) of rh IL-1ß|
|Biological Activity||Measured in a cell proliferation assay using murine D10G4.1 cells. The ED50 for this effect is typically 2-10 pg/ml.|
|Reconstitution||The lyophilized rh IL-1ß is soluble in water and most aqueous buffers and can be reconstituted in water to a concentration of 0.1 mg/ml. This solution can be diluted into other buffered solutions or stored at -20°C for future use.|
|Stability and Storage||Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.|
|Synonyms||IL1B; IL-1; IL1F2; IL1-BETA|
|Description||Interleukin-1 beta (IL-1beta) is produced by activated macrophages. IL-1beta stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1beta proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1 is a name that designates two pleiotropic cytokines, IL-1 alpha (IL1F1) and IL1 beta (IL1F2), which are the products of distinct genes. IL- 1 alpha and IL-1 beta are structurally related polypeptides that share approximately 21% amino acid (aa) identity in human. Both proteins are produced by a wide variety of cells in response to inflammatory agents, infections, or microbial endotoxins. While IL-1 alpha and IL-1 beta are regulated independently, they bind to the same receptor and exert identical biological effects. The human IL-1 beta cDNA encodes a 269 aa precursor. A 116 aa propeptide is cleaved intracellularly by the cysteine protease IL-1 beta converting enzyme (Caspase1/ICE) to generate the active cytokine. The mature human IL-1 beta shares 96% aa sequence identity with rhesus and 67% 78% with canine, cotton rat, equine, feline, mouse, porcine, and rat IL-1 beta. Human recombinant IL-1beta produced in E. coli is a non-glycosylated, IL-1 beta polypeptide chain containing 153 amino acids and having a molecular mass of 17.0 kDa.|
- Proinflammatory cytokines induce rapid, NO-independent apoptosis, expression of chemotactic mediators and interleukin-32 secretion in human pluripotent stem cell-derived beta cells. R. Dettmer et al., Diabetologia. 2022; 65(5): 829–843.
- Osmotic and hypoxic induction of osteopontin in retinal pigment epithelial cells: Involvement of purinergic receptor signaling. M. Hollborn et al., Mol Vis. 2020; 26: 188–203.
- Th22 Cells Promote Osteoclast Differentiation via Production of IL-22 in Rheumatoid Arthritis. Miyazaki Y. et al., Front Immunol. 2018 Dec 10;9:2901.
- Regulation of the hyperosmotic induction of aquaporin 5 and VEGF in retinal pigment epithelial cells: Involvement of NFAT5. M. Hollborn et al., Mol Vis. 2015; 21: 360–377.
- Mutant p53 gains new function in promoting inflammatory signals by repression of the secreted interleukin-1 receptor antagonist. Ubertini V et al., Oncogene. 2015 May 7;34(19):2493-504.
- IL-17 Inhibits Chondrogenic Differentiation of Human Mesenchymal Stem Cells. M. Kondo et al., PLoS One. 2013; 8(11): e79463.
- Identification of a Novel Bacterial Outer Membrane Interleukin-1Β-Binding Protein from Aggregatibacter actinomycetemcomitans. A. Paino et al., PLoS One. 2013; 8(7): e70509.
- Trimeric Form of Intracellular ATP Synthase Subunit β of Aggregatibacter actinomycetemcomitans Binds Human Interleukin-1β. A. Paino et al., PLoS One. 2011; 6(4): e18929.
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