Monoclonal Anti-FAP antibody produced in mouse

Fibroblast activation protein (FAP) is a type II transmembrane serine protease and a cell surface antigen. It is encoded by the gene mapped to human chromosome 2q24.2. FAP is present as a homodimeric integral protein with dipeptidyl peptidase IV like fold. The encoded protein has an α/β-hydrolase domain and an eight-bladed β-propeller domain. It is not expressed in normal tissues. FAP is only expressed by activated fibroblasts in response to pathologic situations.

The protein encoded by this gene 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. (provided by RefSeq)

FAP (AAH26250, 525 a.a. ~ 624 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
PPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWS

Fibroblast activation protein (FAP) is expressed in several pathogenic sites including cancer, fibrosis, arthritis, wounding, or inflammation. FAP has in vitro dipeptidyl peptidase activity and collagenolytic activity. It cleaves N-terminal dipeptides from polypeptides and can degrade gelatin and type I collagen.

Solution in phosphate buffered saline, pH 7.4

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