Human IL-1 Beta ELISA Kit

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Cat: abs510002

Size: 96T

Human IL-1 beta ELISA Kit

Testing Principle

This particular kit employs a sandwich enzyme immunoassay technique, which is quantitative in nature. The high affinity plate is pre-coated with a specific anti-human IL-1 beta antibody. To begin the analysis, standards, test samples, and biotinylated detection antibodies are added to the wells of the enzyme-labeled plate. The incubation time allows for the IL-1 beta present in the samples to combine with the solid-phase antibodies and the detection antibodies, forming immune complexes. Unbound material is then washed away before horseradish peroxidase-labeled streptavidin (HRP) is added. To complete the process, a chromogenic substrate is added and the color is developed in the dark. Addition of a stop solution halts the reaction, and the absorbance at a wavelength of 450 nm (reference correction wavelength of 540 nm or 570 nm) is measured. Overall, this kit is an accurate and reliable method for detecting human IL-1 beta.

Detection type: sandwich enzyme immunoassay

Form: pre-coated 96-well plate

Sample type: Cell culture supernatant, Serum, Plasma

Sample quantity: 100ul

Kit composition:

This package includes a 96-well polystyrene microplate that has been coated with a capture antibody, along with a standard and a detection antibody. It also comes with 10×reagent diluent, color reagents A and B, 25×wash buffer, stop solution, and ELISA plate sealers. All necessary specifications have been provided.

Sensitivity: 1.0 pg / mL

Detection range:  3.9 - 250 pg/mL

Recovery rate: 85-107%

Storage: 2-8 ° C

The standard curve:

Background: IL-1 Beta

The interleukin-1 (IL-1) protein family comprises IL-1α, IL-1β, IL-18, IL-33, and IL-1F5-F10. IL-1α and IL-1β share the same cell-surface binding receptor and have similar biological functions. Under normal conditions, IL-1 is not produced in unstimulated cells in healthy individuals, except in certain cells like skin keratinocytes, some epithelial cells, and some central nervous system cells. However, the expression of IL-1 drastically increases in macrophages and other cell types when exposed to inflammatory factors, infections, or microbial endotoxins. IL-1β plays a crucial role in immune and inflammatory responses, as well as in bone remodeling, fever regulation, carbohydrate metabolism, and GH/IGF-1 physiology. Several diseases are linked to the dysregulation or delayed expression of IL-1, including sepsis, rheumatoid arthritis, inflammatory bowel disease, acute and chronic myeloid leukemia, insulin-dependent diabetes mellitus, atherosclerosis, nerve injury, and age-related conditions.

IL-1α and IL-1β are polypeptides that share approximately 25% homology at the amino acid level. They are both initially synthesized as 31kDa precursors and are then cleaved to produce mature proteins of around 17.5kDa. The cleavage of IL-1β precursor by Caspase-1/ICE is a crucial step in the inflammatory response. Interestingly, neither IL-1α nor IL-1β contains a typical hydrophobic signaling peptide, yet there is evidence suggesting that they can still be secreted extracellularly through non-classical pathways. It has been observed that untreated IL-1α can be found displayed on cell membranes, potentially retaining its biological activity. On the other hand, IL-1β precursors exhibit minimal to no biological activity compared to mature IL-1β. Both the precursors and the mature form of IL-1β are transported out of the cell.

Il-1 and IL-1 exert their effects by binding to IL-1RA through immunoglobulin superfamily receptors.Type I transmembrane receptor (IL-1RI) of 80kDa is expressed in a variety of cells, including T cells, fibroblasts, keratinocytes, endothelial cells, synovial lining cells, chondrocytes, and hepatocytes.Type II transmembrane receptor (IL-1RII) of 68kDa is expressed in B cells, neutrophils, and bone marrow cells.The extracellular domains of IL-1RI and IL-1RII share 28% homology.

But other regions were significantly different. The intracellular domain of type II receptors contained only 29 amino acids, while the intracellular domain of type I receptors contained 213 amino acids. IL-1RII does not seem to respond to IL-1 signals, and its function is to act as a decoy receptor to impair IL-1.IL-1 receptor ligand protein (IL-1RAcP) interaction with IL-1RI is necessary for IL-1RI signaling.IL-1RA is a secretory molecule and a competitive inhibitor of IL-1.Soluble IL-1RI and IL-1RII are present in human plasma, joint fluid, and conditioned medium of several cell lines. In addition, vaccinia virus encodes IL-1 binding proteins similar to soluble IL-1RII.

Technical hints: For research use only, not for in vitro diagnosis.

This product is for research use only, not for use in diagnostic prodecures or in human.

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