Interleukin 17 (also known as CTLA-8) is a T cell-expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of herpesvirus Saimiri. cDNA clones encoding IL-17 have been isolated from activated rat, mouse and human T cells. Human IL-17 cDNA encodes a 155 amino acid (aa) residue precursor protein with a 19 amino acid residue signal peptide that is cleaved to yield the 136 aa residue mature IL-17 containing one potential N-linked glycosylation site. Both recombinant and natural IL-17 have been shown to exist as disulfide linked homodimers. At the amino acid level, human IL-17 shows 72% and 63% sequence identity with herpesvirus and rat IL-17, respectively. An IL-17 specific mouse cell surface receptor (IL-17 R) has recently been cloned. While the expression of IL-17 mRNA is restricted to activated T cells, the expression of mIL-17 R mRNA has been detected in virtually all cells and tissues tested. IL-17 exhibits multiple biological activities on a variety of cells including the induction of IL-6 and IL-8 production in fibroblasts, the enhancement of surface expression of ICAM-1 in fibroblasts, activation of NF-kappaB and costimulation of T cell proliferation.
Molecular Weight:
Approximately 31.0 kDa, disulfide-linked homodimer of two 136 amino acid polypeptide chains.
Source:
Escherichia coli.
Purity:
>95% by SDS-PAGE and HPLC analyses.
Form:
Sterile Filtered White lyophilized (freeze-dried) powder.
Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.
Application Notes:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20C. Further dilutions should be made in appropriate buffered solutions.
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