A recombinant fragment of human SERPINB5 protein (within amino acids 1-200) was used as the immunogen for the SERPINB5 antibody.
Maspin is structurally a serine protease inhibitor (serpin) that was initially isolated from normal human mammary epithelial cells. Serpins are a family of proteins that inhibit Chymotrypsin-like serine proteinases. Serpins control activated proteinases and several are involved in the regulation of cell death. Maspin is found in the extracellular matrix and at the plasma membrane. Maspin has been shown to act at the cell surface to block cell motility and inhibit invasion of breast and prostate cancer cells. Maspin is present in normal mammary epithelial cells but is absent in many tumor cell lines, yet no major structural alterations of the Maspin gene have been identified in tumor cells. Similarly, Maspin is expressed in normal prostate cells and downregulated or absent in prostate tumor cells.
