What are IL-17 cells?

Interleukin-17 (IL-17, also known as IL-17A) is a key cytokine that links T cell activation to neutrophil mobilization and activation. As such, IL-17 can mediate protective innate immunity to pathogens or contribute to the pathogenesis of inflammatory diseases, such as psoriasis and rheumatoid arthritis.

What is the function of IL-17?

Interleukin-17 (IL-17) induces the production of granulocyte colony-stimulating factor (G-CSF) and chemokines such as CXCL1 and CXCL2 and is a cytokine that acts as an inflammation mediator.

What is the difference between IL-17A and IL-17F?

Despite the large number of double- positive cells in these models, IL-17F is dispensable for autoimmune tissue inflammation whereas IL-17A-deficient mice show reduced disease (Ishigame et al., 2009).

Does Th17 produce IL-17?

Th17 cells produce IL-17, IL-17F, and IL-22, thereby inducing a massive tissue reaction owing to the broad distribution of the IL-17 and IL-22 receptors. Th17 cells also secrete IL-21 to communicate with the cells of the immune system.

Which is the ELISA assay for Hu IL-17A?

The Human Interleukin-17A (Hu IL-17A) ELISA quantitates Hu IL-17A in human serum, plasma, buffered solution, or cell culture medium. The assay will exclusively recognize both natural and recombinant Hu IL-17A.

Where did the discovery of IL 17A come from?

IL-17A, often referred to as IL-17, was originally discovered at transcriptional level by Rouvier et al. in 1993 from a rodent T-cell hybridoma, derived from the fusion of a mouse cytotoxic T cell clone and a rat T cell lymphoma.

How is the quantikine human IL 17 immunoassay performed?

No significant interference observed with available related molecules. The Quantikine Human IL-17 Immunoassay is a 4.5 hour solid phase ELISA designed to measure human IL-17 in cell culture supernates, serum, and plasma. It contains E. coli-expressed recombinant human IL-17 and antibodies raised against the recombinant factor.

How many KdA does IL-17 / 17A have?

Human IL-17/17A is synthesized as a 155 amino acid (aa) precursor that contains a 23 aa signal sequence and a 133 aa mature region that possesses a cysteine-knot fold (4-6). In both human and mouse, there is one conserved N-linked glycosylation site that likely contributes 5 kDa to its native molecular weight.