• Biotinylated Human FAP on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.
  • The purity of Biotinylated Human FAP is greater than 95% as determined by SEC-HPLC.
  • Immobilized Anti-FAP Antibody at 5 Mu g/ml (100 Mu l/well) on the plate. Dose response curve for Biotinylated Human FAP, His Tag with the EC50 of 0. 14 Mu g/ml determined by ELISA.

Human FAP protein (Recombinant) (N-His-Avi) {Biotin} (STJP001716)

SKU:
STJP001716

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Host: HEK293
Note: STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Recombinant-Human FAP-N-His-Avi protein was developed from hek293 and has a target region of N-His-Avi. For use in research applications.
Conjugation: Biotin
Formulation: Lyophilised from 0.2 µm filtered PBS solution pH7.4.
Dilution Range: Upon receipt centrifuge vial to ensure maximal product extraction, recommended: 20sec, 5K RPM
Storage Instruction: The lyophilized protein is stable for at least 1 year from date of receipt at-20°C.
Endotoxin: Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg).
Gene Symbol: FAP
Gene ID: 2191
Uniprot ID: SEPR_HUMAN
Immunogen Region: Leu26-Asp760
Immunogen: DNA sequence encoding Human FAP including a N-His-Avi tag was expressed in HEK293 Cells. The recombinant protein was then biotinylated site specific using the AVItag biotinylation technology.
Post Translational Modifications N-glycosylated. The N-terminus may be blocked.
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.
Protein Name 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
Simp
Surface-Expressed Protease
Seprase Cleaved Into - Antiplasmin-Cleaving Enzyme Fap - Soluble Form
Apce
Cellular Localisation Prolyl Endopeptidase Fap: Cell Surface
Cell Membrane
Single-Pass Type Ii Membrane Protein
Cell Projection
Lamellipodium Membrane
Invadopodium Membrane
Ruffle Membrane
Membrane
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
Antiplasmin-Cleaving Enzyme Fap
Soluble Form: Secreted
Found In Blood Plasma And Serum
Isoform 2: Cytoplasm
Alternative Protein Names Prolyl Endopeptidase Fap protein
170 Kda Melanoma Membrane-Bound Gelatinase protein
Dipeptidyl Peptidase Fap protein
Fibroblast Activation Protein Alpha protein
Fapalpha protein
Gelatine Degradation Protease Fap protein
Integral Membrane Serine Protease protein
Post-Proline Cleaving Enzyme protein
Serine Integral Membrane Protease protein
Simp protein
Surface-Expressed Protease protein
Seprase Cleaved Into - Antiplasmin-Cleaving Enzyme Fap - Soluble Form protein
Apce protein
FAP protein

Information sourced from Uniprot.org

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