Recombinant Human FAP Protein Standard (His tag)
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Recombinant Human FAP Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.
View 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
- sELISA
Supplier Data
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.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human FAP Protein Standard (His tag) (AB316637)
SDS-PAGE analysis of ab316637 under reducing conditions for 2ug protein.
Reactivity data
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Why is this recommended?
We recommend this product because it’s often used in the same experiment or related research.
We advise that you always check the datasheet to ensure it fits your experiments, or contact ourtechnical teamfor help.
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
General info
Function
The protein expressed by the FAP gene is a cell surface glycoprotein serine protease involved in the degradation of the extracellular matrix (ECM) and various cellular processes such as tissue remodeling, fibrosis, wound healing, inflammation, and tumor growth. It exists in both plasma membrane-bound and soluble forms, exhibiting post-proline cleaving endopeptidase activity, specifically targeting Ala/Ser-Gly-Pro-Ser/Asn/Ala sequences in substrates like alpha-2-antiplasmin SERPINF2 and SPRY2. FAP protein degrades gelatin and heat-denatured type I collagen but not native type I and IV collagens, nor vitronectin, tenascin, laminin, fibronectin, fibrin, or casein. It also has dipeptidyl peptidase activity, hydrolyzing prolyl bonds when the penultimate residue is proline, with a preference for sequences such as Ala-Pro and Gly-Pro. It acts on natural neuropeptides like neuropeptide Y, peptide YY, substance P, and brain natriuretic peptide 32. In its membrane form, in association with DPP4, PLAUR, or integrins, FAP is involved in pericellular ECM proteolysis, promoting cell adhesion, migration, invasion, and plays roles in development, wound healing, and cell invasiveness in malignant melanoma. It supports tumor progression by facilitating angiogenesis, collagen degradation, apoptosis, and reducing immune response. Additionally, it promotes glioma cell invasion by degrading brevican and functions as a tumor suppressor in melanocytic cells by regulating cell proliferation and survival independently of its serine protease activity. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the peptidase S9B family.
Post-translational modifications
N-glycosylated.. The N-terminus may be blocked.
Target data
Product promise
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