Recombinant Human FAP Protein (N-8His)
Beta LifeScience
SKU/CAT #: BL-2517NP

BL-2517NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Recombinant Human FAP Protein (N-8His)
Beta LifeScience
SKU/CAT #: BL-2517NP
Collections: High-quality recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Prolyl endopeptidase FAP is produced by our Mammalian expression system and the target gene encoding Leu26-Asp760 is expressed with a 8His tag at the N-terminus. |
Accession | Q12884 |
Synonym | FAP; FAPA; DPPIV; SIMP; Fapalpha |
Gene Background | FAP (also known as seprase) is a single-pass type II membrane protein which belongs to thepeptidase S9B family. FAP appears to act as a proteolytically active 170-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. FAP is also an endopeptidase that can degrade Gelatin, Collagens I and IV, Fibronectin, and Laminin as well as several peptide hormones. The enzymatic activity is dependent on FAP association with DPPIV on the cell surface. The matrix-dedgrading activity of FAP contributes to tumor cell migration and invasion. In addition, FAP can enhance tumor cell growth by limiting the development of anti-tumor immunity. |
Molecular Mass | 86.1 KDa |
Apmol Mass | 85-100 KDa, reducing conditions |
Formulation | Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 20% Glycerol, pH 8.0. |
Endotoxin | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
Purity | Greater than 95% as determined by reducing SDS-PAGE. (QC verified) |
Biological Activity | Not tested |
Reconstitution | |
Storage | Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles. |
Shipping | The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below. |
Usage | For Research Use Only |
Target Details
Target Function | Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane 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, vitronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has 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 membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling 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 system. 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. |
Subcellular Location | [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.; [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted.; [Isoform 2]: Cytoplasm. |
Protein Families | Peptidase S9B family |
Database References | HGNC: 3590 OMIM: 600403 KEGG: hsa:2191 STRING: 9606.ENSP00000188790 UniGene: PMID: 30383930 |