Transforming Growth Factor-β1 Latency Associated Peptide human

Research Area: Cell Signaling

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.

Transforming Growth Factor-β1 Latency Associated Peptide human has been used to coat the cell culture inserts for cell migration assays to determine the functional effects of impeding αvβ6 endocytosis in vitro. It has also been used to coat non-tissue culture-treated 96-well plates for adhesion assays.

Latency Associated Peptide (LAP) binds transforming growth factor-beta 1 (TGF-β1) to form a latent complex. The activity of TGF-β1 is primarily regulated through the activation of the latent molecule. LAP has the ability to stimulate epithelial cell migration, representing a new function for LAP in controlling monocyte trafficking and immune modulation. Following post-translational modification, TGF-β1 binds non-covalently to the LAP to establish latency. Due to its crucial function in modulating TGF-β1 activity, LAP plays a fundamental role in governing a range of TGF-β1 effects. LAP is expressed on immature dendritic cells and contributes to T cell differentiation. LAP exhibits both chemotactic and anti-inflammatory activity independently of active TGF-β1.

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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