ELISA Research
Why tissue samples do not need to be activated when TGF- beta (transforming growth factor - beta) was detected;
Source: Elabscience®Published: Mar 08,2024
Since the antibodies in the kit recognize activated TGF-β, and
TGF-β is a disulfide bond linked by two identical or similar 12.5kDa subunits of molecular weight. The study of human TGF-β cDNA sequence showed that the 112 amino acid residues of the monomer TGF-β were cleaved from the carboxyl terminal by a precursor molecule (per-pro-TGF-β) containing 400 amino acid residues. The N-terminal of per-pro-TGF-β contains a signal peptide, which is cleaved before secretion to become an inactive polypeptide chain precursor (pro-TGF-β). The n-terminal part of the amino acid residue is removed by changing the ionic strength, acidification or protease hydrolysis, and the remaining carboxyl terminal part forms an active TGF-β.
A variety of cells in the body can secrete TGF-β in an inactive state. In vitro, the inactive TGF-β, also known as latency associated peptide (LAP), can be activated by acidification. In vivo, the acidic environment can be present near fractures and healing wounds, and the cleavage of the protein itself can cause the TGF-β complex to become activated TGF-β. In general, tissues with active cell differentiation often contain high levels of TGF-β, such as osteoblasts, kidney, bone marrow, and fetal liver hematopoietic cells.
Therefore, no additional activation processing is required for tissue sample testing.