Description_x000D_ General description_x000D_ 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._x000D_ Application_x000D_ Latency Associated Peptide (LAP) may be used to inhibit transforming growth factor-β 1 activity in various biological systems._x000D_ Biochem/physiol Actions_x000D_ 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._x000D_ Physical form_x000D_ Lyophilized from 0.2 μm filtered phosphate buffered saline containing 1.25 mg bovine serum albumin._x000D_ Analysis Note_x000D_ The biological activity is measured by its ability to inhibit TGF-β1 activity on mouse HT-2 cells._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.