Mouse Fibroblast Activation Protein  alpha /FAP Alexa Fluor® 488-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Fibroblast Activation Protein alpha/FAP

FAP (also known as Seprase) is a 95 kDa Type II transmembrane serine protease that is structurally related to dipeptidyl peptidase IV (DPPIV/CD26) (1, 2). Within the extracellular domain, mouse FAP shares 90% and 97% amino acid (aa) sequence identity with human and rat FAP, respectively (3, 4). Alternative splicing of mouse FAP generates isoforms with a 33 aa or 5 aa deletion in the extracellular juxtamembrane region (3). FAP is expressed on reactive stromal fibroblasts in tumor tissue and wound healing and on synoviocytes in rheumatoid arthritis (1, 5-7). It exhibits dipeptidyl peptidase activity with substrate specificity similar to DPPIV, which is specific for N-terminal Xaa-Pro sequences (5, 8). FAP is also an endopeptidase that can degrade Gelatin, Collagens I and IV, Fibronectin, and Laminin (1, 5, 8) as well as several peptide hormones (e.g. Neuropeptide Y, Brain Natriuretic Peptide, Substance P, Peptide YY, and Incretins) (9). The enzymatic activity is dependent on FAP association with DPPIV on the cell surface (5, 8, 10, 11). The matrix-dedgrading activity of FAP contributes to tumor cell migration and invasion (10-13). In addition, FAP can enhance tumor cell growth by limiting the development of anti-tumor immunity (14).

Product Datasheets

Related Research Areas

• Cancer Biomarkers
• DPPIV Family
• Other Putative Cancer Biomarkers
• Search Bioprocessing Enzymes
• Search Immunotherapy-related Enzymes
• Serine Proteases and Regulators