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Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWTransforming growth factor β1 (TGF-β1) is a multifunctional cytokine and member of the TGF-β superfamily.1,2 It is an extracellular dimeric protein that is produced by multiple cell types, including macrophages, platelets, neutrophils, regulatory T cells, and renal tubular cells, and is the most abundantly expressed isoform of TGF-β. TGF-β1 is expressed as a proprotein that is cleaved in the Golgi to form TGF-β1 latency-associated peptide (LAP) and mature TGF-β1.2 TGF-β1 LAP and TGF-β1 remain non-covalently bound until mature TGF-β1 is released from latency by various proteins, including matrix metalloproteinases and plasmin, to regulate immune function, epithelial-mesenchymal transition, and cell proliferation. TGF-β1 LAP inhibits TGF-β1-induced inflammation and fibrosis in HSC-T6 rat hepatic cells and H9c2 rat cardiomyocytes, as well as in a mouse model of carbon tetrachloride-induced liver fibrosis.3,4 Cayman’s TGF-β1 LAP (human, recombinant) protein consists of 260 amino acids, has a calculated molecular weight of 29.9 kDa, and a predicted N-terminus of Leu30 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is ~38-45 kDa due to glycosylation.
WARNING This product is not for human or veterinary use.
1. TGF-
2. TGF-
3. Recombinant truncated latency-
4. Prokaryotic expression, purification and evaluation of anti-