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The protein encoded by MARCKS is a substrate for protein kinase C. De plus, nous expédions MARCKS Kits (22) et MARCKS Protéines (7) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 248 products:
Chinese Hamster Polyclonal MARCKS Primary Antibody pour WB - ABIN152966
Zhang, Ahmed, McFarlane, Capone, Boreham, Truant, Igdoura, Trigatti: Regulation of SR-BI-mediated selective lipid uptake in Chinese hamster ovary-derived cells by protein kinase signaling pathways. dans Journal of lipid research 2007
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Human Polyclonal MARCKS Primary Antibody pour IF, WB - ABIN362996
Litherland, Elias, Hui, Macdonald, Catterall, Barter, Farren, Jefferson, Rowan: Protein kinase C isoforms zeta and iota mediate collagenase expression and cartilage destruction via STAT3- and ERK-dependent c-fos induction. dans The Journal of biological chemistry 2010
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Human MARCKS Primary Antibody pour IHC - ABIN966535
Pariser, Herradon, Ezquerra, Perez-Pinera, Deuel: Pleiotrophin regulates serine phosphorylation and the cellular distribution of beta-adducin through activation of protein kinase C. dans Proceedings of the National Academy of Sciences of the United States of America 2005
The results indicated MARCKS may be the missing link in the regulation of the function (i.e., sodium transport) of epithelial sodium channels by anionic phospholipids.
ENaC (Montrer SCNN1A Anticorps) activity is regulated by calpain-2 (Montrer CAPN2 Anticorps) proteolysis of MARCKS.
In the absence of Pin1 (Montrer PIN1 Anticorps), MARCKS is hyper-phosphorylated, leading to loss of cell adhesions, and collapse of the growth cone.
Findings suggest that MIR429 modulates mucin (Montrer SLC13A2 Anticorps) secretion in human colorectal cells and mouse colitis tissues by up-regulating of MARCKS expression.
Conditional deletion of MARCKS in ECs induces intracellular accumulation of mucins, elevated oxidative stress, and lipid droplet buildup.
MARCKS acts as a "molecular switch," binding to and regulating PIP2 signaling to regulate processes like proplatelet extension (microtubule-driven) vs proplatelet branching (Arp2/3 and actin polymerization-driven).
MARCKS knockdown arrested VSMC cell cycle by decreasing KIS (Montrer UHMK1 Anticorps) expression. Decreased KIS (Montrer UHMK1 Anticorps) expression resulted in nuclear trapping of p27kip1 (Montrer CDKN1B Anticorps) in VSMCs.
MARCKS regulates the expression of proinflammatory cytokines in macrophages through activation of p38 (Montrer CRK Anticorps)/JNK (Montrer MAPK8 Anticorps) MAPK (Montrer MAPK1 Anticorps) and NF-kappaB (Montrer NFKB1 Anticorps).
Targeting phospho-MARCKS overcomes drug-resistance and induces antitumor activity in preclinical models of multiple myeloma.
Grin 1 (Montrer GPRIN1 Anticorps) is identified as a novel Cdk5 (Montrer CDK5 Anticorps) substrate and MARCKS is confirmed as a Cdk5 (Montrer CDK5 Anticorps) substrate.
MARCKS appears to be a nonessential regulatory protein in mast cell exocytosis but exerts a negative modulation.
Marcksb is required for proper gastrulation movements of zebrafish.
data suggest a major contribution of MARCKS to kidney cancer growth and provide an alternative therapeutic strategy of improving the efficacy of multikinase inhibitors.
These data suggested that miR34c3p acts as a tumor suppressor via regulation of MARCKS expression in OS progression
Ca(2+)-PKC-MARCKS-PIP2-PI3K-PIP3 system functions as an activation module in vitro
Findings show that calmodulin (CaM) stimulates phosphoinositide-3-kinase (PI3K) lipid kinase activity by binding MARCKS and displacing it from phosphatidylinositol 4,5-bisphosphate (PIP2) headgroups, thereby releasing free PIP2 that recruits active PI3K to the membrane and serves as the substrate for the generation of phosphatidylinositol 3,4,5-trisphosphate (PIP3).
Knockdown of MARCKS in HepG2 cells reduced cell migration and invasion, but not cell proliferation.
MARCKS upregulation increases vascular smooth muscle cell motility by activation of Rac1 and Cdc42 (Montrer CDC42 Anticorps), promoting neointima formation.
A novel role for MARCKS in regulating nuclear functions such as gene expression.
unresponsiveness of breast cancer to paclitaxel treatment is, at least in part, mediated by phospho-MARCKS
MARCKS protein mediates hydrogen peroxide regulation of endothelial permeability.
a critical role for H(2)O(2) in angiotensin-II signaling to the endothelial cytoskeleton in a novel pathway that is critically dependent on MARCKS, Rac1, and c-Abl.
These findings demonstrate a critical role for MARCKS-phosphatidylinositol-4,5-diphosphate signaling in regulating dendrite development.
Protein kinase C (Montrer PKC Anticorps) mediated inhibition of endothelial L-arginine (Montrer GATM Anticorps) transport is mediated by MARCKS protein
The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.
myristoylated alanine-rich protein kinase C substrate
, methyl binding domain
, myristoylated alanine-rich C-kinase substrate
, Myristoylated alanine-rich protein kinase C substrate
, protein kinase C substrate 80 kDa protein
, myristoylated alanine-rich protein kinase C substrate (MARCKS, 80K-L)
, protein kinase C substrate, 80 kDa protein, light chain
, myristoylated alanine-rich C kinase substrate (MARCKS)