Detection of Rat IL‑6 by Western Blot. Western blot shows lysates of NR8383 rat alveolar macrophage cell line untreated (-) or treated (+) with LPS. PVDF membrane was probed with 1 µg/mL of Goat Anti-Rat|
IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF506) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for IL‑6 at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
|IL‑6 in Mouse T Cells. IL‑6 was detected in immersion fixed activated mouse T Cells using 15 µg/mL Rat IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF506) for 3 hours at room temperature. Cells were stained (red) and counterstained (green). View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
Cell Proliferation Induced by IL‑6 and Neutralization by Rat IL‑6 Antibody. Recombinant Rat IL‑6 (Catalog # 506-RL) stimulates proliferation in the T118.104.22.168 mouse plasmacytoma cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Rat|
IL‑6 (0.6 ng/mL) is neutralized (green line) by increasing concentrations of Rat IL‑6 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF506). The ND50 is typically 0.1-0.5 µg/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 central to 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 rat IL-6 is 187 amino acids (aa) in length and shares 41% and 85% aa sequence identity with human and mouse IL-6, respectively (5). 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 (6). gp130 is also a component of the receptors for CLC, CNTF, CT-1, IL-11, IL-27, LIF, and OSM (7). 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, 8).
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