Porcine IL-1 Beta ELISA Kit

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Cat: abs540002

Size: 96T

Porcine IL-1 beta ELISA Kit

Testing Principle

The technique employed in this kit is a quantitative sandwich enzyme immunoassay. A plate with a high affinity is coated with a specific anti-porcine IL-1 beta antibody. To the wells of the plate, standards, test samples, and biotinylated detection antibodies are added. Following an incubation period, the IL-1 beta in the samples binds with the solid-phase antibodies and detection antibodies, creating immune complexes. Unbound materials are washed away, and horseradish peroxidase-labeled streptavidin (HRP) is introduced. After another round of washing, a chromogenic substrate is added, and the color develops in a dark environment. To halt the reaction, a stop solution is applied, and the absorbance is measured at 450 nm, with a reference correction 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:

The specification for the 96-well polystyrene microplate includes the presence of a capture antibody coating. It also contains a standard and a detection antibody. The diluent for the reagent is provided at a concentration of 10 times. To initiate the color reaction, two color reagents, A and B, are included. A concentrated wash buffer is provided at a 25 times concentration to ensure effective washing of the plate. Finally, a stop solution is included to terminate the reaction. Additionally, the package includes ELISA plate sealers for convenient sealing of the microplate.

Sensitivity: 3.8 pg/mL

Detection range:  62.5 - 4,000 pg/mL

Recovery rate: 69-102%

Storage: 2-8 ° C

The standard curve:

Background: IL-1 Beta

The interleukin-1 (IL-1) protein family comprises various members, including IL-1α and IL-1β. Likewise, IL-1 receptor antagonists (IL-1RA), IL-18, IL-33, and IL-1F5-F10, and IL-1α and IL-1β have the same receptor binding capability and comparable biochemical functions. In healthy individuals, unstimulated cells do not produce IL-1, except for some central nervous system cells, skin keratinocytes, and certain epithelial cells. However, the expression of IL-1 sharply increases in response to inflammatory factors, infections, or endotoxins in many cell types, particularly macrophages. Among its various functions, IL-1β is critical in regulating immune and inflammatory responses, bone remodeling, fever, carbohydrate metabolism, and GH/IGF-1 physiology. Several dysfunctions, including delayed expression or dysregulation in IL-1, are associated with numerous diseases such as sepsis, rheumatoid arthritis inflammatory bowel disease, type 1 diabetes, atherosclerosis, nerve injuries, and age-related ailments.

IL-1α and IL-1β are polypeptides that share structural similarities, exhibiting approximately 25% homology at the amino acid level. These polypeptides are initially produced as larger 31kDa precursors, which are subsequently cleaved to yield smaller, mature proteins of approximately 17.5kDa in size. The cleavage of the IL-1β precursor by an enzyme called Caspase-1/ICE plays a crucial role in triggering the inflammatory response. Interestingly, neither IL-1α nor IL-1β possesses a typical hydrophobic signaling peptide, yet there is evidence suggesting their ability to be secreted extracellularly through non-classical pathways. In the case of IL-1α, the untreated portion can be exhibited on the cell membranes and may retain its biological activity. On the other hand, the IL-1β precursor exhibits minimal to no biological activity compared to its mature counterpart. Nonetheless, both the IL-1β precursors and mature IL-1β are capable of being 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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