ARG70823
Human FAP / Fibroblast activation protein recombinant protein (Active) (His-tagged, C-ter)
Human FAP / Fibroblast activation protein recombinant protein (Active) (His-tagged, C-ter) for SDS-PAGE
Overview
| Product Description | CHO expressed, His-tagged (C-ter) Active Human FAP / Fibroblast activation protein recombinant protein |
|---|---|
| Tested Application | SDS-PAGE |
| Target Name | FAP / Fibroblast activation protein |
| Species | Human |
| A.A. Sequence | Leu26 - Asp761 |
| Expression System | CHO |
| Activity | Active |
| Activity Note | Determinedd by its ability to bind human FAP Antibody in functional ELISA. Immobilized Recombinant human FAP Protein can bind human FAP Antibody. |
| Alternate Names | Fibroblast activation protein alpha; SIMP; Seprase; Integral membrane serine protease; Surface-expressed protease; EC 3.4.21.26; Dipeptidyl peptidase FAP; 170 kDa melanoma membrane-bound gelatinase; EC 3.4.14.5; APCE; Serine integral membrane protease; DPPIV; EC 3.4.21.-; FAPalpha; Gelatine degradation protease FAP; Post-proline cleaving enzyme; Prolyl endopeptidase FAP; FAPA |
Properties
| Form | Powder |
|---|---|
| Purification Note | Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test. |
| Purity | > 95% (by SDS-PAGE) |
| Buffer | PBS (pH 7.4) |
| Reconstitution | It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 200 μg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely. |
| Storage Instruction | For long term, lyophilized protein should be stored at -20°C or -80°C. After reconstitution, aliquot and store at -20°C or -80°C for up to one month. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. |
| Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
| Gene Symbol | FAP |
|---|---|
| Gene Full Name | fibroblast activation protein, alpha |
| Background | The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014] |
| 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, 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 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. [UniProt] |
| Cellular Localization | 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. [UniProt] |
| PTM | N-glycosylated. The N-terminus may be blocked. [UniProt] |
