|Detection of Human Fibroblast Activation Protein alpha /FAP by Western Blot. Western blot shows lysates of WI‑38 human lung fibroblast cell line. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human Fibroblast Activation Protein alpha /FAP Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF3715) followed by Streptavidin-HRP (Catalog # DY998). A specific band was detected for Fibroblast Activation Protein alpha /FAP at approximately 97 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
FAP (also known as seprase) is a Type II transmembrane serine protease that is structurally related to dipeptidyl peptidase IV (1). FAP has substrate specificity similar to dipeptidyl peptidase IV, which is specific for N-terminal Xaa-Pro sequences, but FAP is also an endopeptidase able to degrade gelatin and Type I collagen (2). The enzymatically active form of FAP is a dimer (3). FAP has a restricted tissue distribution. It is not detectable in normal tissues or resting fibroblasts, but is highly expressed on reactive stromal fibroblasts in epithelial cancers (4), in granulation tissue during wound healing, and in bone and soft tissue sarcomas (5). Because of its expression patterns and enzymatic activities, FAP is believed to play roles in tumor invasion, tissue remodeling, and wound repair.
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