FAP Protein, Human (HEK293, N-His)

The FAP protein is a cell surface glycoprotein serine protease that is critical for extracellular matrix degradation and plays multiple roles in tissue remodeling, fibrosis, wound healing, inflammation, and tumor growth. FAP Protein, Human (HEK293, His) is the recombinant human-derived FAP protein, expressed by HEK293 , with N-8*His labeled tag.

FAP protein, a cell surface glycoprotein serine protease, plays a crucial role in extracellular matrix degradation and is involved in diverse cellular processes, including tissue remodeling, fibrosis, wound healing, inflammation, and tumor growth. Both the plasma membrane and soluble forms of FAP exhibit post-proline cleaving endopeptidase activity, demonstrating a preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences on substrates such as alpha-2-antiplasmin SERPINF2 and SPRY2. FAP can degrade gelatin, heat-denatured type I collagen, and various other substrates. Additionally, it possesses dipeptidyl peptidase activity, hydrolyzing prolyl bonds in synthetic dipeptide substrates with a preference for specific amino acid sequences. In association with DPP4, PLAUR, or integrins, the plasma membrane form of FAP participates in pericellular proteolysis of the extracellular matrix, promoting cell adhesion, migration, and invasion. FAP's multifaceted functions extend to tissue remodeling during development and wound healing. In malignant melanoma cancers, FAP enhances cell invasiveness towards the extracellular matrix and promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. While contributing to tumor growth progression by increasing angiogenesis, collagen fiber degradation, and apoptosis, FAP paradoxically acts as a tumor suppressor in melanocytic cells through the regulation of cell proliferation and survival in a serine protease activity-independent manner.

Measured by its ability to convert the substrate benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin (HY-D1670) to Z-Gly-Pro and 7-amino-4-methylcoumarin (HY-D0027) that incubate at room temperature in kinetic mode for 5 minutes. The specific activity is 39796.92 pmol/min/μg.

Human

HEK293

N-8*His

Q12884-1 (L26-D760)

2191

LRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD

Approximately 85-100 kDa due to the glycosylation.

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose, 5% mannitol and 0.01% Tween80.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.