Mouse IL-1 Beta ELISA Kit

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Cat: abs520001

Size: 96T

Mouse IL-1 beta ELISA Kit

Testing Principle

This particular kit employs a quantitative sandwich enzyme immunoassay technique. To begin with, a plate with a high affinity has been coated with a specific anti-mouse IL-1 beta antibody. In the next step, both standards and test samples are added to the wells of the enzyme-labeled plate, along with biotinylated detection antibodies. Following a period of incubation, the IL-1 beta found in the samples binds with the solid-phase antibodies and the detection antibodies, forming immune complexes. To eliminate any excess or unbound material, a thorough washing process is carried out. Subsequently, horseradish peroxidase-labeled streptavidin (HRP) is introduced and allowed to bind. After another round of washing, a chromogenic substrate is introduced to the mixture, leading to the development of a distinct color in a dark environment. Finally, the reaction is brought to a halt by adding a stop solution, and the resulting absorbance is measured at a wavelength of 450 nm. It's worth noting that the measurement is corrected using a reference wavelength of either 540 nm or 570 nm.

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 is coated with a capture antibody, a standard, and a detection antibody. Also included are a 10x reagent diluent, color reagents A and B, a 25x wash buffer, and a stop solution to complete the ELISA assay. You will also receive ELISA plate sealers and a specification with detailed instructions for use.

Sensitivity: 3.8 pg/mL

Detection range:  15.6 - 1,000 pg/mL

Recovery rate: 69-102%

Storage: 2-8 ° C

The standard curve:

Background: IL-1 Beta

The IL-1 protein family comprises several members, namely IL-1α, IL-1β, IL-1 receptor antagonists (IL-1RA), IL-18, IL-33, and IL-1F5-F10. IL-1α and IL-1β share a cell-surface binding receptor and exhibit comparable biological functions. Normally, unstimulated cells in healthy individuals do not produce IL-1, except for certain cells such as skin keratinocytes, some epithelial cells, and certain cells within the central nervous system. However, the expression of IL-1 significantly increases in macrophages and other cell types in response to inflammatory factors, infections, or microbial endotoxins.
IL-1β plays a crucial role in immune and inflammatory responses, as well as various physiological processes including bone remodeling, fever regulation, carbohydrate metabolism, and GH/IGF-1 physiology. Dysregulation or delayed expression of IL-1 is associated with numerous diseases such as sepsis, rheumatoid arthritis, inflammatory bowel disease, acute and chronic myeloid leukemia, insulin-dependent diabetes mellitus, atherosclerosis, nerve injury, and age-related diseases.

Both IL-1α and IL-1β are polypeptides that share a structural similarity of approximately 25% at the amino acid level. They are initially synthesized as 31kDa precursors and then cleaved to form mature proteins of around 17.5kDa. The cleavage of IL-1β precursor by Caspase-1/ICE is a crucial step in the inflammatory response. Despite the absence of a typical hydrophobic signaling peptide, there is evidence suggesting that both IL-1α and IL-1β can be secreted extracellularly through non-classical pathways. Interestingly, the untreated portion of IL-1α can be displayed on cell membranes while still 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 mature forms 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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