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The protein encoded by MST1 contains four kringle domains and a serine protease domain, similar to that found in hepatic growth factor. Additionally we are shipping MST1 Antibodies (102) and MST1 Proteins (15) and many more products for this protein.
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In the present study, we investigated the expression of activated core Hippo pathway kinases (pMST1/2 and pLATS1/2) in a series of 57 HER2 (show ERBB2 ELISA Kits)-positve and triple-negative breast cancer patients who received neoadjuvant therapy .
Mst1-induced defective mitophagy evoked cellular oxidative stress, energy metabolism and calcium overload. Through excessive mitochondrial fission and aberrant mitophagy, Mst1 launched caspase 9-related mitochondrial apoptosis and abrogated F-actin/lamellipodium-dependent cellular migration.
These data suggest that MSP (show MSMB ELISA Kits) is an effective inhibitor of inflammation and lipid accumulation in the stressed liver, thereby indicating that MSP (show MSMB ELISA Kits) has a key regulatory role in non-alcoholic steatohepatitis.
Study found that MST1 is strongly activated in a diabetic beta cell and induces not only its death but also directly impairs insulin (show INS ELISA Kits) secretion through promoting proteasomal degradation of key beta cell transcription factor, pancreatic and duodenal homeobox 1 (PDX1 (show PDX1 ELISA Kits)), which is critical for insulin (show INS ELISA Kits) production.
deacetylation of MST1 mediated by HBXIP-enhanced HDAC6 results in MST1 degradation in a chaperone-mediated autophagy (CMA) manner in promotion of breast cancer growth.
Mst1 increases the (show FOXP3 ELISA Kits)acetylation of Foxp3 by inhibiting Sirt1 activity, which requires the Mst1 kinase activity.
Identify MST1/MSP as a mitogen for tracheal basal cells.
MSP (show MSMB ELISA Kits) appears to promote the migration of fibroblasts, enhances collagen synthesis and remodeling, and effectively improves wound healing.
Elevated serum levels of MST1 were found in subjects with excessive alcohol use.
results suggest that the decreased expression of MST1 in regulatory T cells due to hypermethylation of the promoter contributes to the pathogenesis of IgG4-related AIP (show AIP ELISA Kits)
These data suggest that MSP is an effective inhibitor of inflammation and lipid accumulation in the stressed liver, thereby indicating that MSP has a key regulatory role in non-alcoholic steatohepatitis.
kinases, including Slk (show SLK ELISA Kits), Lok and Mst1, are inhibited by BI-D1870 but to a much lesser extent by BIX 02565 and that phosphorylation of some of their substrates is blocked by BI-D1870 in living cells.
Nicorandil alleviates post-MI cardiac dysfunction and remodeling. The mechanisms were associated with enhancing autophagy and inhibiting apoptosis through Mst1 inhibition.
Using a standard two-thirds partial hepatectomy (PH) model in young and aged mice, the activity of the core kinases MST1 and LATS1 increased during the early hypertrophic phase and returned to steady state levels in the proliferative phase, coinciding with activation of YAP1 (show YAP1 ELISA Kits) target genes and hepatocyte proliferation.
The MST1 acts as a molecular brake to maintain immune tolerance by regulating T cell-mediated B cell activation (show BLNK ELISA Kits).
Mst1 knockout alleviated while Mst1 overexpression aggravated cardiac dysfunction in diabetes.
these findings highlight a role for MST1 in vesicle trafficking and extravasation in neutrophils, providing an additional mechanistic explanation for the severe immune defect
Results identify L-plastin as a key effector of Mst1 and establish a novel mechanism linking a signaling intermediate to an actin-binding protein critical to T cell migration.
MIST1 is a scaling factor necessary and sufficient by itself to induce and maintain secretory cell architecture
Mst1 deficiency diminishes atherosclerosis and stabilizes atherosclerotic plaques in ApoE (show APOE ELISA Kits)(-/-) mice. Mst1 may participate in atherosclerosis progression through inhibition of macrophage autophagy and promotion of macrophage apoptosis.
The protein encoded by this gene contains four kringle domains and a serine protease domain, similar to that found in hepatic growth factor. Despite the presence of the serine protease domain, the encoded protein may not have any proteolytic activity. The receptor for this protein is RON tyrosine kinase, which upon activation stimulates ciliary motility of ciliated epithelial lung cells. This protein is secreted and cleaved to form an alpha chain and a beta chain bridged by disulfide bonds.
hepatocyte growth factor-like protein
, hepatocyte growth factor-like protein homolog
, macrophage-stimulating protein
, E2F transcription factor 2
, macrophage stimulatory protein
, hepatocyte growth factor-like/macrophage stimulating protein
, macrophage stimulating 1 (hepatocyte growth factor-like)
, 12S E1A
, macrophage stimulating 1 L homeolog