Detection Principle:

This kit uses double antibody sandwich enzyme-linked immunosorbent assay technology. Specific anti porcine IL-1-beta; The antibody was pre coated on a high affinity microplate. Add the standard, sample to be tested and biotinylated detection antibody into the wells of the enzyme plate. After incubation, the il-1&beta in the sample; Combine with solid-phase antibody and detection antibody to form immune complexes. After washing to remove unbound material, horseradish peroxidase labeled streptavidin HRP was added. After washing, the chromogenic substrate was added to avoid light for color development. Stop the reaction by adding stop solution, and determine the absorbance value at 450 nm wavelength (refer to the correction wavelength of 540nm or 570nm).

Detection Type: double antibody sandwich method

Form: pre coated 96 well plate

Detection Sample Type: cell supernatant, serum, Plasma

Loading Amount: 100ul

Kit Components:

Precoated 96 well plate, standard, anti porcine il-1β One copy of detection antibody, dilution buffer, chromogenic solution (a, b), washing solution, termination solution, sa-hrp, plate sealing membrane and instructions.

Sensitivity: 3.8 pg/ml

Detection Range: 62.5 - 4000 pg/ml

Recovery Range: 69-102%

Storage Method: 2-8 ℃

Standard Curve

Background:

Interleukin 1 (IL-1)The protein family contains the canonical members il-1&alphaIl-1β And IL-1ra, as well as IL-18, IL-33, and il-1f5-10. Il-1α And il-1β It binds to the same cell surface receptors and shares biological functions. In addition to skin keratinocytes, some epithelial cells, and some cells of the central nervous system, unstimulated cells in healthy mice do not produce IL-1. However, as a response to inflammatory substances, infection or microbial endotoxin, macrophages and many other cells will produce IL-1 in large quantities. In the physiological process of immune response and inflammatory response, bone remodeling, fever, glucose metabolism, growth hormone / IGF-1, il-1β Plays a key role. Under a series of pathological conditions, including sepsis, rheumatoid arthritis, inflammatory bowel disease, acute and chronic myeloid leukemia, insulin-dependent diabetes mellitus, atherosclerosis, nerve injury and aging related diseases, IL-1 has been accompanied by abnormal or continuous production.

IL-1α And il-1β It has structurally related polypeptides with approximately 25% homology at the amino acid level. Both of them were synthesized as 31 kDa sized precursors and then cleaved into mature proteins with a molecular weight of approximately 17.5 kDa. Caspase-1 / ICeI cleaves il-1β Precursors are a key step in the inflammatory response. Il-1α And il-1β None of them contain typical hydrophobic signal peptides, but there is evidence that these factors can be secreted through non canonical pathways. A portion of unprocessed il-1α It can appear on the cell membrane and may have biological activity. With il-1α Different precursors, il-1β The precursors have little biological activity compared with the mature ones. Unprocessed and mature il-1β Can be exported from cells.

IL-1α And il-1β Functions through immunoglobulin superfamily receptors that bind to IL-1ra. Cells expressing 80kDa transmembrane type I receptor (IL-1 RI) include T cells, fibroblasts, keratinocytes, endothelial cells, synovial fluid inner layer cells, chondrocytes, and hepatocytes. Cells expressing 68kDa transmembrane type II receptor (IL-1 RII) include B cells, neutrophils, and bone marrow cells. The extracellular domains of these two IL-1 receptors share about 28% homology, but the significant difference is reflected in their intracellular domains: the intracellular domain of type II receptor has only 29 amino acids, while the intracellular domain of type I receptor has 217 amino acids. IL-1 RII does not produce signal for IL-1, and may act as a decoy receptor to weaken IL-1 function. IL-1 receptor accessory protein (IL-1 RACP) is associated with IL-1 RI and is required for IL-1RI signal transduction. IL-1ra is a secreted molecule that functions as a competitive inhibitor of IL-1. Soluble IL-1RI and IL-1 RII can be detected in human plasma, synovial fluid and conditioned medium of various human cell lines. In addition, IL-1 binding protein similar to soluble IL-1 RII is able to be encoded by vaccinia and vaccinia virus.