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The protein encoded by ST14 is an epithelial-derived, integral membrane serine protease. Additionally we are shipping Suppression of Tumorigenicity 14 (Colon Carcinoma) Kits (8) and Suppression of Tumorigenicity 14 (Colon Carcinoma) Proteins (7) and many more products for this protein.
Showing 10 out of 104 products:
Human Polyclonal ST14 Primary Antibody for CyTOF, FACS - ABIN4900442
Sales, Masedunskas, Bey, Rasmussen, Weigert, List, Szabo, Overbeek, Bugge: Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndrome. in Nature genetics 2010
Show all 12 Pubmed References
Human Polyclonal ST14 Primary Antibody for IP, WB - ABIN250689
Désilets, Longpré, Beaulieu, Leduc: Inhibition of human matriptase by eglin c variants. in FEBS letters 2006
Show all 6 Pubmed References
Human Monoclonal ST14 Primary Antibody for CyTOF, FACS - ABIN4900443
Zoratti, Tanabe, Varela, Murray, Bergum, Colombo, Lang, Molinolo, Leduc, Marsault, Boerner, List: Targeting matriptase in breast cancer abrogates tumour progression via impairment of stromal-epithelial growth factor signalling. in Nature communications 2015
Show all 3 Pubmed References
Human Monoclonal ST14 Primary Antibody for ELISA - ABIN520529
Sasaroli, Gimotty, Pathak, Hammond, Kougioumtzidou, Katsaros, Buckanovich, Devarajan, Sandaltzopoulos, Godwin, Scholler, Coukos: Novel surface targets and serum biomarkers from the ovarian cancer vasculature. in Cancer biology & therapy 2011
limited role for HAI-2 (show SPINT2 Antibodies) in the inhibition of matriptase and prostasin (show PRSS8 Antibodies) is the result of its primarily intracellular localization in basal and spinous layer keratinocytes, which probably prevents the Kunitz inhibitor from interacting with active prostasin (show PRSS8 Antibodies) or matriptase
Abrogation of matriptase expression by silencing with RNAi or inhibition of matriptase proteolytic activity with a synthetic inhibitor impairs the conversion of inactive pro-HGF to active HGF and subsequent c-Met-mediated signaling.
Data, including data from studies using cadaver tissue, suggest that matriptase and matriptase mRNA are expressed in several regions of the brain with an enrichment in neurons; higher levels of matriptase RNA are expressed in young individuals as compared to older individuals; matriptase cleaves amyloid beta precursor protein at a specific arginine residue (Arg-102).
Activation of proHGF by St14 induces mouse embryonic stem cell differentiation.
The authors report that ST14/Prss14 is an emerging therapeutic target for breast cancer where HER2 (show ERBB2 Antibodies) is not applicable.
These results identify EpCAM (show EPCAM Antibodies) as a substrate of matriptase and link HAI-2 (show SPINT2 Antibodies), matriptase, EpCAM (show EPCAM Antibodies), and claudin-7 (show CLDN7 Antibodies) in a functionally important pathway that causes disease when it is dysregulated.
Matriptase is present in macrophages from patients with mutated alpha-1 antitrypsin (show SERPINA1 Antibodies) at high levels and contributes to their proteolytic activity on extracellular matrix. MMP-14 (show MMP14 Antibodies) is a novel substrate for matriptase, which regulates the levels of MMP-14 (show MMP14 Antibodies) on the cell surface. High levels of matriptase may contribute to increased ECM (show MMRN1 Antibodies) degradation by Z-M, both directly and through MMP-14 (show MMP14 Antibodies) activation.
Ultraviolet irradiation/reactive oxygen species induced matriptase proteolysis may have short term protective effects and contribute to the recovery from acute epidermal damage and/or pathology of skin with chronic sun damage.
The present study demonstrated that ovarian cancer cell metastasis and invasion were more dependent on upregulation of matriptase levels than downregulation of HAI1 (show SPINT1 Antibodies). Matriptase may be a potential adjuvant therapeutic target for inhibiting ovarian cancer invasion and metastasis.
Given that matriptase-1 participates in terminal KC differentiation, its absence in psoriatic skin lesions indicates that this contributes to the barrier disturbances in this disease.
The proliferation impairment in matriptase-deficient breast cancer cells is caused by their inability to initiate activation of the c-Met signalling pathway in response to fibroblast-secreted pro-HGF (show HGF Antibodies).
Matriptase is a critical promoter of late stages of squamous cell carcinoma progression and induces pro-tumorigenic chemokine (show CCL1 Antibodies) and cytokine release, and inflammatory cell accumulation in established tumors.
Data show that proteinase-activated receptor (PAR)-2-dependent inflammatory signaling as an essential component of matriptase-mediated and potentiation of ras-mediated oncogenesis.
HAI-1 (show SPINT1 Antibodies) regulates the activity of activated matriptase, whereas HAI-2 (show SPINT2 Antibodies) has an essential role in regulating prostasin (show PRSS8 Antibodies)-dependent matriptase zymogen activation.
Our results reveal unexpected complementary roles of matriptase-prostasin (show PRSS8 Antibodies)- and PAR-2 (show F2RL1 Antibodies)-dependent proteolytic signaling in the establishment of placental epithelial barrier function and overall embryonic survival.
These findings suggest that TGF-beta (show TGFB1 Antibodies) induces epithin/PRSS14 shedding by mediating translocation of epithin/PRSS14 sheddase, TACE (show ADAM17 Antibodies), to the membrane.
Matriptase deletion initiates a Sjogren's syndrome-like disease in mice.
Matriptase is required for the active form of hepatocyte growth factor (show HGF Antibodies) induced Met, focal adhesion kinase and protein kinase B (show AKT1 Antibodies) activation on neural stem/progenitor cell motility.
ST14 expression is downregulated in colitis.
The protein encoded by this gene is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.
membrane-type serine protease 1
, serine protease 14
, serine protease TADG-15
, suppression of tumorigenicity 14 (colon carcinoma, matriptase, epithin)
, suppressor of tumorigenicity 14 protein
, tumor associated differentially expressed gene 15 protein
, tumor-associated differentially-expressed gene 15 protein
, matriptase a
, suppression of tumorigenicity 14 (colon carcinoma) a
, suppressor of tumorigenicity 14 protein homolog
, suppressor of tumorigenicity protein 14
, protease, serine, 14 (epithin)
, membrane-type serine protease