Recombinant Human FAP Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293, with >=80% purity and suitable for sELISA, SDS-PAGE.
Images
Key facts
- Purity
- >=80% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- His tag C-Terminus
- Applications
- sELISA, SDS-PAGE
- Biologically active
- No
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application sELISA | Reactivity Reacts | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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 (PubMed:14751930, PubMed:16223769, PubMed:16410248, PubMed:16480718, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711, PubMed:2172980, PubMed:7923219, PubMed:9065413). 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 (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16410248, PubMed:16651416, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). 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.
Alternative names
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, FAPalpha, SIMP, Seprase, FAP
Recommended products
Recombinant Human FAP Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293, with >=80% purity and suitable for sELISA, SDS-PAGE.
Key facts
- Purity
- >=80% SDS-PAGE
- Expression system
- HEK 293 cells
- Tags
- His tag C-Terminus
- Applications
- sELISA, SDS-PAGE
- Biologically active
- No
- Accession
- Q12884-1
- Animal free
- Yes
- Species
- Human
- Concentration
- Storage buffer
pH: 7.3 - 7.5
Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic
Sequence info
Amino acid sequence
- Accession
- Q12884
- Protein length
- Fragment
- Predicted molecular weight
- 86.6 kDa
- Nature
- Recombinant
- Tags
- His tag C-Terminus
Specifications
- Form
- Liquid
General info
- 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 (PubMed:14751930, PubMed:16223769, PubMed:16410248, PubMed:16480718, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711, PubMed:2172980, PubMed:7923219, PubMed:9065413). 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 (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16410248, PubMed:16651416, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). 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.
- Sequence similarities
Belongs to the peptidase S9B family.
- Post-translational modifications
N-glycosylated.
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Notes
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
FAP also known as fibroblast activation protein alpha or seprase is a serine protease with a mass of approximately 97 kDa. It is largely expressed in embryonic tissues certain carcinomas and tissue remodeling sites. FAP acts mechanistically by exhibiting dipeptidyl peptidase and endopeptidase activities breaking down peptide chains. Cellular membrane-bound FAP localizes mainly on reactive stromal fibroblasts not normal tissues making it an interesting target for research.
- Biological function summary
FAP plays a role in tissue remodeling and wound healing influencing the microenvironment of tumors and fibrotic tissues. It contributes to extracellular matrix degradation participating in the complex network of proteases. FAP is not a standalone unit but part of a larger complex that interacts with other proteases helping in cell migration and invasion. As a result its activity impacts processes like inflammation and carcinogenesis.
- Pathways
FAP participates in processes related to tissue repair and cancer progression. Significant pathways include the degradation of the extracellular matrix and the PI3K/AKT signaling. It functions alongside proteins like DPP4 another dipeptidyl peptidase in these pathways. The matrix breakdown is central to cancer metastasis and wound healing enhancing our understanding of FAP's role in larger biological contexts.
- Associated diseases and disorders
FAP has links with cancer and fibrosis. Its expression correlates with aggressive tumors and poor prognosis in cancers such as breast and ovarian. In fibrotic diseases like pulmonary and liver fibrosis it contributes to excessive matrix deposition and tissue stiffening. FAP's involvement alongside collagenases in these disorders makes it a target of potential therapeutic interest.
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2 product images
SDS-PAGE - Recombinant Human FAP Protein Standard (His tag) (ab316637)
SDS-PAGE analysis of ab316637 under reducing conditions for 2ug protein.
Sandwich ELISA - Recombinant Human FAP Protein Standard (His tag) (ab316637)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
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