Description_x000D_ General description_x000D_ Fibroblast activation protein alpha (FAPa) is a type II transmembrane serine protease. It is present as a homodimeric integral protein with dipeptidyl peptidase IV like fold. It has an α/β-hydrolase domain and an eight-bladed β-propeller domain. It is not expressed in normal tissue. It is only expressed by activated fibroblast in response to pathologic situations. It is expressed in several pathogenic sites including cancer, fibrosis, arthritis, wounding, or inflammation._x000D_ Application_x000D_ FAPa may be used to study the role in coordinating the stromal response to cancer, in angiogenesis, and modulation of the antitumor immune response._x000D_ Biochem/physiol Actions_x000D_ FAPα has in vitro dipeptidyl peptidase activity and collagenolytic activity. It cleaves N-terminal dipeptides from polypeptides and can degrade gelatin and type I collagen. It has also been reported that FAPa has a tumor suppressor activity._x000D_ FAP is a Type II transmembrane serine protease which has substrate specificity for prolyl peptides bonds (Pro-Xaa). This endopeptidase cleaves gelatin and is believed to play a role in tissue remodeling, tumor invasion, and wound repair._x000D_ Unit Definition_x000D_ One unit will convert 1 picomole of benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin (ZP-AMC) to Z-gly-Pro and 7-amino-4-methylcoumarin (AMC) per minute at pH 7.5 at 25°C._x000D_ Physical form_x000D_ Supplied as a solution in 25 mM Tris, 0.25 M NaCl and 20% (v/v) glycerol , pH 8.0