TGF-β is released from degranulating platelets and secreted from nearly all cells in a biologically inactive complex which is unable to bind to cellular receptors and is not recognized by antibodies to TGF-β. The peptide can be activated by acidification, alkalinization, or action of chaotropic agents in vitro. The complex consists of TGF-β associated non-covalently with a protein designated as the latency associated peptide (LAP). TGF-β and LAP represent components of a pro-peptide that is cleaved in a post-golgi compartment prior to secretion. The recombinant human LAP is produced from a DNA sequence corresponding to the 278 amino acid residues of pre-pro-TGF-β1 terminating prior to the mature TGF-β1. LAP contains a Cys33 to Ser33 substitution. LAP contains 249 amino acids, generated after cleavage of a 29 amino acid residue signal peptide. LAP is a glycoslyated, disulfide linked homodimer.
Latency Associated Peptide (LAP) may be used to inhibit transforming growth factor-β 1 activity in various biological systems.
TGF-β1 is produced by many cell types, but is reported to be most concentrated in mammalian platelets, where it is present at approximately four times the level of TGF-β2.
Lyophilized from 0.2 μm filtered phosphate buffered saline containing 1.25 mg bovine serum albumin.
The biological activity is measured by its ability to inhibit TGF-β1 activity on mouse HT-2 cells.
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