SpecificityBy ELISA and immunoblotting, the antibody shows < 5% cross-reactivity with rhIL1 alpha, rmIL1 beta.
In addition the antibody shows no cross-reactivity with rmIl1 alpha, rhIL1 ralpha, rmIL1 ralpha, and rrIL1 ralpha.
The antibody will not neutralize the biological activity of rhIL1 alpha, rmIL1 alpha or rmIL1 beta.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution.
Use at an assay dependent dilution. Predicted molecular weight: 31 kDa.
Use at an assay dependent dilution.
FunctionPotent 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.
Tissue specificityExpressed in activated monocytes/macrophages (at protein level).
Sequence similaritiesBelongs to the IL-1 family.
Post-translational modificationsActivation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated.
Cellular localizationCytoplasm, 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 (PubMed:24201029). 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 (PubMed:15192144). 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 (PubMed:24201029). 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 (PubMed:11728343). 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.
References for Anti-IL1 beta antibody [8516.311] (ab10749)
This product has been referenced in:
Lucchesi W et al. Differential gene regulation by Epstein-Barr virus type 1 and type 2 EBNA2. J Virol82:7456-66 (2008).
Read more (PubMed: 18480445) »
Pioli PA et al. Lipopolysaccharide-induced IL-1 beta production by human uterine macrophages up-regulates uterine epithelial cell expression of human beta-defensin 2. J Immunol176:6647-55 (2006).
Read more (PubMed: 16709823) »