Mouse IL-1 beta/IL-1F2 Quantikine HS ELISA Kit Summary
Sample Type & Volume Required Per Well
Serum (50 uL), EDTA Plasma (50 uL), Heparin Plasma (50 uL)
0.8 - 50 pg/mL (Serum, EDTA Plasma, Heparin Plasma)
Natural and recombinant mouse IL-1 beta
< 0.5% cross-reactivity observed with available related molecules.< 50% cross-species reactivity observed with species tested.
No significant interference observed with available related molecules.
The Quantikine® HS Mouse IL-1 beta /IL-1F2 Immunoassay is a 4.0 hour solid phase ELISA designed to measure mouse IL-1 beta levels in serum and plasma. It contains E.
coli-expressed recombinant mouse IL-1 beta and antibodies raised against the recombinant protein. Results obtained using natural IL-1 beta showed linear curves that were parallel to the standard curves obtained using the Quantikine® HS kit standards. These results indicate that the Quantikine® HS Immunoassay kit can be used to determine relative mass values for natural mouse IL-1 beta.
Intra-Assay Precision (Precision within an assay) <div>Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.</div>
Inter-Assay Precision (Precision between assays) <div>Three samples of known concentration were tested in twenty separate assays to assess inter-assay precision. Assays were performed by at least three technicians.</div>
Serum, EDTA Plasma, Heparin Plasma
The recovery of mouse IL-1 beta spiked to levels throughout the range of the assay in various matrices was evaluated.
||Average % Recovery
|EDTA Plasma (n=4)
|Heparin Plasma (n=4)
To assess the linearity of the assay, samples spiked with high concentrations of mouse IL-1 beta were serially diluted with calibrator diluent to produce samples with values within the dynamic range of the assay.
Mouse IL-1 beta /IL-1F2 Standard Curve
Preparation and Storage
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Background: IL-1 beta/IL-1F2
The Interleukin 1 (IL-1) family of proteins consists of
IL-1 alpha, IL-1 beta, and the IL-1 receptor antagonist (IL-1ra). IL-1 alpha and IL-1 beta bind
to the same cell surface receptors and share biological functions (1). 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 seen. 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,
insulindependent diabetes mellitus, atherosclerosis, neuronal injury, and
aging-related diseases (2-5).
IL-1 alpha and IL-1 beta are structurally related polypeptides that
show approximately 25% homology at the amino acid (aa) level. Both are
synthesized as 31 kDa precursors that are subsequently cleaved into mature
proteins of approximately 17.5 kDa (6, 7). Cleavage of the IL-1 beta precursor by
Caspase-1/ICE is a key step in the inflammatory response (2, 8). Neither IL-1 alpha
nor IL-1 beta contains a typical hydrophobic signal peptide (9-11), but evidence
suggests that these factors can be secreted by non-classical pathways (12, 13).
A portion of unprocessed IL-1 alpha can be presented on the cell membrane and may
retain biological activity (14). 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 (13, 15). 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 (16,
17). The 68 kDa transmembrane type II receptor (IL-1 RII) is expressed on B cells,
neutrophils, and bone marrow cells (18). 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
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 (19). The IL-1 receptor accessory protein (IL-1
RAcP) associates with IL-1 RI and is required for IL-1 RI signal transduction
(20). IL-1ra is a secreted molecule that functions as a competitive inhibitor
of IL-1 (21, 22). 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 (23, 24). In addition, IL-1 binding proteins that resemble soluble
IL-1 RII are encoded by vaccinia and cowpox viruses (25).
Interleukin 1 beta
Entrez Gene IDs:
3553 (Human); 16176 (Mouse); 24494 (Rat); 397122 (Porcine); 403974 (Canine); 100034237 (Equine); 100135556 (Guinea Pig)
catabolin; IL1 beta; IL-1 beta; IL-1; IL1B; IL-1b; IL1-BETA; IL-1F2; IL1F2IL-1 beta; interleukin 1, beta; interleukin-1 beta; preinterleukin 1 beta; pro-interleukin-1-beta