Fibroblast Activation Protein Alpha (FAPa)

APCE; SIMP; DPPIV; Seprase; 170 kDa melanoma membrane-bound gelatinase; Post-proline cleaving enzyme; Serine integral membrane protease; Surface-expressed protease

Fibroblast Activation Protein Alpha (FAPa)

Fibroblast activation protein, alpha, also known as FAP, is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. FAP, also known as seprase, belongs to the clan SC proteases and is a member of the S9B prolyl oligopeptidase subfamily. Other members of the S9B subfamily are DPPIV, DPP8 and DPP9. FAP is most closely related to DPPIV and they share about 50% of there amino acids.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)