Cathepsin D, Human

USA

-80

Cathepsin D, also known as CTSD and CPSD, belongs to the peptidase A1 family. Cathepsin D is an aspartic protease that becomes activated at a pH of 5 in hepatocyte endosomes where it degrades insulin. In addition to low pH, activation of cathepsin D depends critically on protonation of its Asp active site residue. .Asp-protonation and low pH leads to a conformational switch in cathepsin-D where the N terminal segment of the protease moves out of the active site. Cathepsin D can be cleaved into the following 2 chains: cathepsin D light chain and cathepsin D heavy chain, which is expressed in the aorta extracellular space. Cathepsin D plays a role in antigen processing, cell proliferation and tissue renewal, and prohormone activation.
Recombinant Human Cathepsin D produced in CHO cells is a polypeptide chain containing 402 amino acids. A fully biologically active molecule, rh Cathepsin D has a molecular mass of 44 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.