Recombinant Human IL-10 Protein, CF Summary
Ser19-Asn178, with a N-terminal Met
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 100-500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Measured in a cell proliferation assay using MC/9‑2 mouse mast cells. The ED50 for this effect is 0.075-0.750 ng/mL.
2 μg/lane of Recombinant Human IL‑10 Protein (Catalog # 1064-ILB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 18.4 kDa.
Interleukin 10, also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL‑10 family of alpha ‑helical cytokines that also includes IL‑19, IL‑20, IL‑22, IL‑24, and IL‑26/AK155 (1, 2). IL‑10 is secreted by many activated hematopoietic cell types as well as hepatic stellate cells, keratinocytes, and placental cytotrophoblasts (2-5). Mature human IL‑10 shares 72%-86% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat IL‑10. Whereas human IL‑10 is active on mouse cells, mouse IL‑10 does not act on human cells (6, 7). IL‑10 is a 178 amino acid molecule that contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer (6, 8, 9). The IL‑10 dimer binds to two IL‑10 R alpha /IL‑10 R1 chains, resulting in recruitment of two IL‑10 R beta /IL‑10 R2 chains and activation of a signaling cascade involving JAK1, TYK2, and STAT3 (10). IL‑10 R beta does not bind IL‑10 by itself but is required for signal transduction (1). IL‑10 R beta also associates with IL‑20 R alpha, IL‑22 R alpha, or IL‑28 R alpha to form the receptor complexes for IL‑22, IL‑26, IL‑28, and IL‑29 (11-13). IL‑10 is a critical molecule in the control of viral infections and allergic and autoimmune inflammation (14-16). It promotes phagocytic uptake and Th2 responses but suppresses antigen presentation and Th1 proinflammatory responses (2).
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