Catalog Number: C22-101-17 Source: Escherichia coli. Molecular Weight: Approximately 31.0 kDa, disulfide-linked homodimer of two 132 amino acid polypeptide chains. Quantity: 5μg/25μg/1000μg AA Sequence: GITIPRNPGC PNSEDKNFPR TVMVNLNIHN RNTNTNPKRS SDYYNRSTSP WNLHRNEDPE RYPSVIWEAK CRHLGCINAD GNVDYHMNSV PIQQEILVLR REPPHCPNSF RLEKILVSVG CTCVTPIVHH VA Purity: >95% by SDS-PAGE and HPLC analyses. Biological Activity: Fully biologically active when compared to standard. The ED50 determined by inducing IL-6 secretion of murine NIH/3T3 cells is less than 7.5 ng/ml, corresponding to a specific activity of > 1.3 × 105 IU/mg. Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Formulation: Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4. Endotoxin: Less than 1EU/μg of rHuIL-17 as determined by LAL method. Reconstitution: 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 <-20°C. Further dilutions should be made in appropriate buffered solutions. Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles. Usage: This material is offered by Shanghai Corning Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. .
Human Interleukin-17 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 (a.a.) residue precursor protein with a 19 amino acid residue signal peptide that is cleaved to yield the 136 a.a. 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-κB and costimulation of T cell proliferation.
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