Biolegend, 594509, Recombinant Mouse Latent TGF-β (ELISA Std.)

Latent TGF-β is secreted as a complex consisting of LAP and TGF-β1. LAP and TGF-β1 are synthesized as a single propeptide precursor of 390 amino acids with an N-terminal signal peptide of 29 amino acids, a 249 amino acids pro-region (LAP), and a 112 amino acids C-terminal region (TGF-β1). Both LAP and TGF-β1 exist as homodimers in circulation, but the disulfide linked homodimers of LAP and TGF-β1 remain non-covalently associated, forming the small latent TGF-β complex (SLC, 100 kD). The large latent TGF-β complex (LLC, 235-260 kD) contains a third component, the latent TGF-β binding protein (LTBP), which is linked to LAP by a single disulfide bond. LTBP does not confer latency but is for efficient secretion of the complex to extracellular sites. TGF-β1 and LAP can be released (activated) by many factors, including enzymes and low or high pH. TGF-β1 and LAP have multiple functions, such as regulating proliferation and differentiation of various cell types. Increased production and activation of latent TGF-β have been linked to immune defects associated with malignancy and autoimmune disorders, to susceptibility to opportunistic infection, and to the fibrotic complications associated with chronic inflammatory conditions. Latent TGF-β has been found to protect against glomerulonephritis. It is a surface marker of activated regulatory T cells.