Human IL-8/CXCL8 ELISA Kit

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Cat: abs510004

Size: 96T

Human IL-8/CXCL8 ELISA Kit

Testing Principle

This particular kit employs a quantitative sandwich enzyme immunoassay technique. It features a high affinity plate that has been pre-coated with a specific anti-human IL-8 antibody. The procedure involves adding standards, test samples, and biotinylated detection antibodies to the wells of the enzyme-labeled plate. Following an incubation period, the IL-8 present in the samples combines with the solid-phase antibodies and the detection antibodies to create immune complexes. These complexes are then washed to remove any unbound material before introducing horseradish peroxidase-labeled streptavidin (HRP). After another round of washing, a chromogenic substrate is added, resulting in the development of color in a dark environment. To stop the reaction, a stop solution is added, and the absorbance is measured at a wavelength of 450 nm. It's worth noting that a reference correction wavelength of either 540 nm or 570 nm is also used in this process.

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 includes a 96-well polystyrene microplate that has been coated with a capture antibody. It also includes a standard, a detection antibody, a 10× reagent diluent, and color reagents A and B. Additionally, there is a 25× wash buffer and a stop solution. To ensure proper sealing of the ELISA plate, it comes with plate sealers.

Sensitivity: 7.8 pg / mL

Detection range:  31.2 - 2000 pg/mL

Recovery rate: 96-118%

Storage: 2-8 ° C

The standard curve:

Background: IL-8

IL-8, or Interleukin-8, is a chemokine that belongs to the alpha or CXC family and is around 8-9 kda in size. It has the ability to bind to heparin and is also known as CP-1, NAP-1, and CXCL8. Human CXC family proteins are quite diverse, with 15 proteins discovered thus far and ranging in size from 8 to 12kDa. These proteins are mostly located on the fourth chromosome of humans, and their structure typically features a triple β fold/an α helix. A common feature of many CXC family proteins is the Glu-Leu-Arg tripeptide sequence at the N-terminal.

The production of human IL-8 involves the creation of a 99 amino acid precursor, with a 20 amino acid signal sequence and a mature region of 79 amino acids. In vivo, IL-8 can exist as a monomer, homologous dimer, or heterodimer with CXCL4/PF4. Among these forms, the IL-8 monomer is thought to exhibit the highest biological activity, while heterodimers may enhance the activity of PF4.
Interestingly, mature human IL-8 displays a significant amount of homology with pigs and dogs, with amino acid similarities of 65% and 70%, respectively. However, the gene for IL-8 has not yet been identified in rodents. Furthermore, multiple subtypes of IL-8 can be produced through selective splicing and proteolysis. Selective splicing can occur at the c-terminal, with an 11-amino acid substitution (position aa#92-99). Meanwhile, cell-specific protease hydrolysis can produce truncation at the N-terminal of IL-8. This process may differ depending on the cell type, with fibroblasts and vascular endothelial cells cutting amino acids 21 and 22 to form IL-8, while monomer cells and lymphocytes cut amino acids 21 to 25 to produce IL-8. Interestingly, these shorter forms of IL-8 tend to have higher biological activity, particularly for CXCR 1 IL-8 receptors.

Citrullination occurs in about 15% of precursor IL-8 at Arg27, which increases the half-life of IL-8 and promotes leukocytosis. IL-8 is secreted by many cell types, including monocytes, neutrophils, fibroblasts and keratinocytes, mast cells, visceral smooth muscle cells, dendritic cells, type II alveolar cells and endothelial cells.

There are two IL-8 receptors, both belonging to G protein-coupled receptor proteins, which are CXCR1/IL-8RA and CXCR2/IL-8RB, with 77% homology in amino acid sequence between them.CXCR1 has a molecular weight of 45-50kDA and is almost completely exclusive to IL-8.CXCR2 has a molecular weight of 35-40kDa and is common to all CXC chemokines. CXCR1 and CXCR2 form constitutive homologous dimers, which seem to be their functional configurations. And when the cell is expressed, heterodimers are also formed. But when it binds to IL-8, it breaks down.CXCR2 responds to low concentrations of IL-8 and is mainly related to chemotaxis and MMP-9 release. In contrast, CXCR1 responds to high concentrations of IL-8 and is associated with respiratory bursts and activation of phospholipase D2.Therefore, CXCR2 is believed to guide neutrophils to migrate to the inflammatory site and then induce CXCR1-mediated antimicrobial activity.

inflammatory site and then induce CXCR1-mediated antimicrobial activity. IL-8 is best known for its pro-inflammatory role in immune cells. Essentially, IL-8 is secreted by a variety of cell types exposed to inflammatory stimulants. For monocytes/macrophages, microbial exposure causes il-8 release. Subsequently, CXCR2-mediated chemokine migrates neutrophils to the site of antigen attack, accompanied by the activation and initiation of the next antimicrobial activity. IL-8 can enhance the action of m-CSF in bone marrow, thus causing the maturation and release of granulocytes. These two functions of IL-8 complement each other.

IL-8 has been reported to have angiogenic effects on tumor-associated endothelial cells. At this point, tumor-derived IL-8 activates CXCR1 and CXCR2 in vascular endothelial cells in a paracrine manner.CXCR1 and CXCR2 are both associated with PI3-K/Akt and RasGTP signaling pathways and are involved in cell survival and proliferation. In addition, IL-8 positively regulates VEGFR2 and EGFR, which are receptor tyrosine kinases that mediate cell growth and migration.

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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