Interleukin-10; Human IL-10, 2ug

IL-10, Interleukin-10, human: Human Interleukin-10 Interleukin 10, also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL-10 family of α-helical cytokines that also includes IL-19, IL-20, IL-22, IL-24, and IL-26/AK155. IL-10 is secreted by many activated hematopoietic cell types as well as hepatic stellate cells, keratinocytes, and placental cytotrophoblasts. Whereas human IL-10 is active on mouse cells, mouse IL-10 does not act on human cells. IL10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. The IL-10 dimer binds to two IL-10 Rα/IL-10R1 chains, resulting in recruitment of two IL-10 Rβ/IL-10R2 chains and activation of a signaling cascade involving JAK1, TYK2, and STAT3. IL-10Rβ does not bind IL-10 by itself but is required for signal transduction. IL-10 is a critical molecule in the control of viral infections and allergic and autoimmune inflammation. It promotes phagocytic uptake and Th2 responses but suppresses antigen presentation and Th1 proinflammatory responses. Source: Escherichia coli. Molecular Weight: Approximately 18.6kDa, a single non-glycosylated polypeptide chain containing 161 amino acids. Quantity: 2ug/10ug/1mg Purity: >95% by SDS-PAGE and HPLC analyses. Biological Activity: Determined by the dose-dependent co-stimulation (with murine IL-4) of MC/9 cells. The ED50 was found to be ≤ 2 ng/ml, corresponding to a specific activity of ≥ 5 x 105 units/mg. Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Formulation: Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.4.  AA Sequence: MSPGQGTQSE NSCTHFPGNL PNMLRDLRDA FSRVKTFFQM KDQLDNLLLKESLLEDFKGY LGCQALSEMI QFYLEEVMPQ AENQDPDIKA HVNSLGENLK TLRLRLRRCH RFLPCENKSK AVEQVKNAFN KLQEKGIYKA MSEFDIFINY IEAYMTMKIR N Endotoxin: Less than 1EU/mg of rHuIL-10 as determined by LAL method.