Recombinant Human Prolyl endopeptidase FAP(FAP),partial

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.

Tris-based buffer, 50% glycerol

Cell surface glycoprotein serine protease that participates in Extracellular domain matrix degradation and involved in many cellular processes including tissue rodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma mbrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma mbrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the Extracellular domain matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue rodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune syst. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.

Repeated freezing and thawing is not recommended. Store working aliquots at 4C for up to one week.

Prolyl endopeptidase FAP: Cell surface, Cell membrane, Single-pass type II membrane protein, Cell projection, lamellipodium membrane, Single-pass type II membrane protein, Cell projection, invadopodium membrane, Single-pass type II membrane protein, Cell projection, ruffle membrane, Single-pass type II membrane protein, Membrane, Single-pass type II membrane protein, Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles, Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix, Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma, Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner, Localized at plasma and ruffle membranes in a collagen-independent manner, Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner, Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner, Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin, SUBCELLULAR LOCATION: Antiplasmin-cleaving enzyme FAP, soluble form: Secreted

FAP

Homo sapiens (Human)