FAP Human
Sf9, Baculovirus cells.
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP
Greater than 90.0% as determined by SDS-PAGE.
Description
FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.
FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP
Sf9, Baculovirus cells.
ADPLRPSRVH NSEENTMRAL TLKDILNGTF SYKTFFPNWI SGQEYLHQSA DNNIVLYNIE TGQSYTILSN RTMKSVNASN YGLSPDRQFV YLESDYSKLW RYSYTATYYI YDLSNGEFVR GNELPRPIQY LCWSPVGSKL AYVYQNNIYL KQRPGDPPFQ ITFNGRENKI FNGIPDWVYE EEMLATKYAL WWSPNGKFLA YAEFNDTDIP VIAYSYYGDE QYPRTINIPY PKAGAKNPVV RIFIIDTTYP AYVGPQEVPV PAMIASSDYY FSWLTWVTDE RVCLQWLKRV QNVSVLSICD FREDWQTWDC PKTQEHIEES RTGWAGGFFV STPVFSYDAI SYYKIFSDKD GYKHIHYIKD TVENAIQITS GKWEAINIFR VTQDSLFYSS NEFEEYPGRR NIYRISIGSY PPSKKCVTCH LRKERCQYYT ASFSDYAKYY ALVCYGPGIP ISTLHDGRTD QEIKILEENK ELENALKNIQ LPKEEIKKLE VDEITLWYKM ILPPQFDRSK KYPLLIQVYG GPCSQSVRSV FAVNWISYLA SKEGMVIALV DGRGTAFQGD KLLYAVYRKL GVYEVEDQIT AVRKFIEMGF IDEKRIAIWG WSYGGYVSSL ALASGTGLFK CGIAVAPVSS WEYYASVYTE RFMGLPTKDD NLEHYKNSTV MARAEYFRNV DYLLIHGTAD DNVHFQNSAQ IAKALVNAQV DFQAMWYSDQ NHGLSGLSTN HLYTHMTHFL KQCFSLSDHH HHHH
Product Science Overview
FAP was first identified in the mid-1980s by Rettig et al. while studying cell surface antigens to characterize activated fibroblasts. They discovered the F19 antigen on epithelial cancer cells, soft tissue sarcomas, granulation tissue of wound healing, and some fetal mesenchymal fibroblasts, naming it “FAP” due to its strong expression on activated fibroblasts . Concurrently, Aoyama and Chen identified a dimeric 170 kDa gelatinase at the invasive front of the human melanoma cell line LOX, which they named "seprase" . Subsequent molecular cloning and protein sequence analysis confirmed that FAP and seprase were identical .
FAP is almost undetectable in normal tissues but is significantly expressed in various pathological conditions, including fibrosis, arthritis, and cancer . It has extensive endonuclease activity and plays a crucial role in degrading the extracellular matrix (ECM), promoting tumor growth, invasion, metastasis, and immunosuppression .
Recombinant human FAP is produced using baculovirus expression systems in Spodoptera frugiperda (Sf21) cells. It is typically supplied as a carrier-free, highly purified protein with a molecular mass of approximately 86 kDa . The recombinant protein is used in various research applications, including studying its enzymatic activities, nonenzymatic functions, and potential as a therapeutic target .
