|Detection of Human IL‑6 by Western Blot. Western blot shows lysates of human peripheral blood mononuclear cells (PBMC) untreated (-) or treated (+) with PHA. PVDF membrane was probed with 0.2 µg/mL of Goat Anti-Human IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-206-NA) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for IL‑6 at approximately 20-22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|IL‑6 in Human PBMCs. IL‑6 was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) treated with LPS and monensin using Goat Anti-Human IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-206-NA) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
|Cell Proliferation Induced by IL‑6 and Neutralization by Human IL‑6 Antibody. Recombinant Human IL‑6 (Catalog # 206-IL) stimulates proliferation in the T122.214.171.124 mouse plasmacytoma cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Human IL‑6 (2.5 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF-206-NA). The ND50 is typically 15-45 ng/mL.|
Interleukin 6 (IL-6) is a pleiotropic alpha -helical cytokine that plays important roles in acute phase reactions, inflammation, hematopoiesis, bone metabolism, and cancer progression. IL-6 activity is essential for the transition from acute inflammation to either acquired immunity or chronic inflammatory disease. It is secreted by multiple cell types as a 22-28 kDa phosphorylated and variably glycosylated molecule (1-4). Mature human IL-6 is 183 amino acids (aa) in length and shares 41% aa sequence identity with mouse and rat IL-6 (5). Alternate splicing generates several isoforms with internal deletions, some of which exhibit antagonistic properties (6-9). Human IL-6 is equally active on mouse and rat cells (10). IL-6 induces signaling through a cell surface heterodimeric receptor complex composed of a ligand binding subunit (IL-6 R) and a signal transducing subunit (gp130). IL-6 binds to IL-6 R, triggering IL-6 R association with gp130 and gp130 dimerization (11). gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM (12). Soluble forms of IL-6 R are generated by both alternate splicing and proteolytic cleavage (3). In a mechanism known as trans-signaling, complexes of soluble IL-6 and IL-6 R elicit responses from gp130-expressing cells that lack cell surface IL-6 R (3). Trans-signaling enables a wider range of cell types to respond to IL-6, as the expression of gp130 is ubiquitous, while that of IL-6 R is predominantly restricted to hepatocytes, leukocytes, and lymphocytes (3). Soluble splice forms of gp130 block trans-signaling from IL-6/IL-6 R but not from other cytokines that utilize gp130 as a coreceptor (4, 13).
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AF-206-NA detects a 20-22 kDa band in lysate in Western blot.