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Validated All-in-One™ qPCR Primer for FAP(NM_004460.4) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
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. [provided by RefSeq].
Gene References into function
- expression of the seprase-DPPIV complex is restricted to migratory cells involved in wound closure
- seprase and the urokinase plasminogen activator receptor (uPAR), co-localize in the plasma membrane of LOX malignant melanoma cells
- This protein and collagen are intrahepatically expressed in hepatitis C infection.
- Seprase may be an early marker of tumor invasion in squamous lesions of the uterine cervix.
- An abundant expression of seprase in colorectal cancer tissue is associated with lymph node metastasis.
- Seprase may contribute to the pathogenesis of breast cancer by promoting growth of the primary tumor and by facilitating the growth of breast cancer cells in metastases at other sites of the body
- These results suggested that there is a difference in seprase expression between intestinal- and diffuse-type gastric cancer; this difference may reflect distinct biological features of these types of cancer
- the enzymatic activity of fibroblast activation protein plays an important role in the promotion of tumor growth
- molecular determinants responsible for the substrate specificity and endopeptidase activity
- analysis of response of CD4(+) and CD8(+) T-cells to the human stromal antigen, fibroblast activation protein
- FAP has important nonenzymatic functions that in chronic liver injury may facilitate tissue remodeling through FAP-mediated enhancement of HSC cell adhesion, migration, and apoptosis
- Increased expression of seprase is associated with lymph node metastasis in colorectal cancer
- Circulating antiplasmin-cleaving enzyme (APCE) has a role in fibrinolysis and appears structurally similar to fibroblast activation protein (APCE).
- Conversion of FAP to the more easily fibrin-incorporable form, Asn-alpha2AP, may increase plasmin inhibition within fibrin
- fibroblast activation protein protease inhibition is based on dipeptide substrate specificity
- FAP required substrates with Pro at P(1) and Gly or d-amino acids at P(2) and preferred small, uncharged amino acids at P(3), but tolerated most amino acids at P(4), P(1)(') and P(2)(').
- Expression of active FAPalpha on chondrocyte membrane and elevated levels in cartilage from osteoarthritis patients. May have important pathological role in cartilage turnover prevalent in arthritic diseases.
- overexpression in HEK293 cells reduced cell adhesion, migration and invasion on ECM components, increased proliferation and promoted apoptosis, independently of enzyme activity
- The reported type 1 diabetes association is from a linkage disequilibrium region including three candidate genes, FAP, IFIH1 and GCA.
- The substrate specificity of FAP was identified by mapping of cleavage sites within collagen I, and peptides synthesized based on these sites showed similar Km values for high and low ranked substrates, but the kcat values differed up to 100-fold.
- FAP-alpha expression in metaplastic, dysplastic, and esophageal cancer tissue is associated with neoplastic progression of esophageal lesions.
- Fibroblast activation protein is highly expressed in pancreatic adenocarcinoma, with greatest expression immediately adjacent to tumor. Higher FAP expression is associated with worse clinical outcome.
- seprase may have a role in promotion of an invasive phenotype by collagenous matrices in ovarian tumor cells
