Key Product Details
Assay Type
Solid Phase Sandwich ELISA
Assay Range
3.91-250 pg/mL
Sample Type
Cell culture supernates, serum, and plasma
Note: Diluents for complex matrices, such as serum and plasma, should be evaluated prior to use in this DuoSet
Human IL-1 beta/IL-1F2 DuoSet ELISA Features
- Optimized capture and detection antibody pairings with recommended concentrations save lengthy development time
- Development protocols are provided to guide further assay optimization
- Assay can be customized to your specific needs
- Economical alternative to complete kits
Other Reagents Required
DuoSet Ancillary Reagent Kit 2 (5 plates): (Catalog # DY008C) containing 96 well microplates, plate sealers, substrate solution, stop solution, plate coating buffer (PBS), wash buffer, and Reagent Diluent Concentrate 2.
PBS: (Catalog # DY006), or 137 mM NaCl, 2.7 mM KCl, 8.1 mM Na2HPO4, 1.5 mM KH2PO4, pH 7.2 - 7.4, 0.2 µm filtered
Wash Buffer: (Catalog # WA126), or equivalent
Reagent Diluent*
Blocking Buffer*
Substrate Solution: ELISA TMB Substrate (Catalog # DY999B or DY999B-250)
Stop Solution: Methanesulfonic acid (Catalog # DY994B or DY994B-250)
Microplates: (Catalog # DY990), or equivalent
Plate Sealers: (Catalog # DY992), or equivalent
*For the recommended Reagent Diluent and Blocking Buffer for a specific DuoSet ELISA Development Kit, refer to the product datasheet.
Background: IL-1 beta/IL-1F2
The Interleukin 1 (IL-1) family of proteins consists of the
classic members IL-1 alpha, IL-1 beta, and IL-1ra, plus IL-18, IL-33 and IL-1F5-F10.
IL-1 alpha and IL-1 beta bind to the same cell surface receptors and share biological
functions. IL-1 is not produced by unstimulated cells of healthy individuals
with the exception of skin keratinocytes, some epithelial cells, and certain
cells of the central nervous system. However, in response to inflammatory
agents, infections, or microbial endotoxins, a dramatic increase in the
production of IL-1 by macrophages and various other cell types is observed.
IL-1 beta plays a central role in immune and inflammatory responses, bone
remodeling, fever, carbohydrate metabolism, and GH/IGF-I physiology.
Inappropriate or prolonged production of IL-1 has been implicated in a variety
of pathological conditions including sepsis, rheumatoid arthritis, inflammatory
bowel disease, acute and chronic myelogenous leukemia, insulin dependent
diabetes mellitus, atherosclerosis, neuronal injury, and aging-related
diseases. IL-1 alpha and IL-1 beta are structurally related polypeptides that
show approximately 25% homology at the amino acid level. Both are synthesized
as 31 kDa precursors that are subsequently cleaved into mature proteins of
approximately 17.5 kDa. Cleavage of the IL-1 beta precursor by Caspase-1/ICE is a
key step in the inflammatory response. Neither IL-1 alpha nor IL-1 beta contains a
typical hydrophobic signal peptide, but evidence suggests that these factors
can be secreted by non-classical pathways. A portion of unprocessed IL-1 alpha can
be presented on the cell membrane and may retain biological activity. The
precursor form of IL-1 beta, unlike the IL-1 alpha precursor, shows little or no
biological activity in comparison to the processed form. Both unprocessed and
mature forms of IL-1 beta are exported from the cell.
IL-1 alpha and IL-1 beta exert their effects through immunoglobulin
superfamily receptors that additionally bind IL-1ra. The 80 kDa transmembrane
type I receptor (IL-1 RI) is expressed on T cells, fibroblasts, keratinocytes,
endothelial cells, synovial lining cells, chondrocytes, and hepatocytes. The 68
kDa transmembrane type II receptor (IL-1 RII) is expressed on B cells,
neutrophils, and bone marrow cells. The two IL-1 receptor types show
approximately 28% homology in their extracellular domains but differ
significantly in that the type II receptor has a cytoplasmic domain of only 29
amino acids (aa), whereas the type I receptor has a 213 aa cytoplasmic domain.
IL-1 RII does not appear to signal in response to IL-1 and may function as a
decoy receptor that attenuates IL-1 function. The IL-1 receptor accessory
protein (IL-1 RAcP) associates with IL-1 RI and is required for IL-1 RI signal
transduction. IL-1ra is a secreted molecule that functions as a competitive
inhibitor of IL-1. Soluble forms of both IL-1 RI and IL-1 RII have been
detected in human plasma, synovial fluids, and the conditioned media of several
human cell lines. In addition, IL-1 binding proteins that resemble soluble IL-1
RII are encoded by vaccinia and cowpox viruses.
Long Name
Interleukin 1 beta
Alternate Names
IL-1b, IL-1F2, IL1 beta, IL1B
Additional IL-1 beta/IL-1F2 Products
Powered by Bioz
