|Detection of Human, Mouse, and Rat MIF by Western Blot. Western blot shows lysates of U937 human histiocytic lymphoma cell line, J774A.1 mouse reticulum cell sarcoma macrophage cell line, and NR8383 rat alveolar macrophage cell line. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human/Mouse MIF Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1978) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for MIF at approximately 12 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
MIF (Macrophage Inhibitory Factor; also GIF) is a 12-13 kDa member of the MIF family of proteins. Although secreted, it possesses no definitive signal sequence. MIF is widely expressed, and serves to regulate immune reactions. On macrophages and B cells, MIF binds to a CD74:CD44 complex, initiating downstream signaling. On monocytes, this promotes TNF-alpha production plus IFN-gamma -stimulated NO production. On B cells, this promotes B cell survival. MIF also binds to leukocyte CD74:CXCR2 and CD74:CXCR4 heterodimers, initiating T cell and monocyte migration. A tautomerase activity has also been shown for MIF, but the significance of this is unclear. Mouse MIF is 114 amino acids (aa) in length. Its tautomerase activity is suggested to involve the entire length of the molecule. MIF is phosphorylated at Ser91, and an additional, singular Cys residue is covalently linked to MIF at Cys60. MIF is considered to act as a homotrimer. Full-length mouse MIF shows 90% and 99% aa sequence identity with human and rat MIF, respectively.
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