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The protein encoded by MARCKS is a substrate for protein kinase C. Zusätzlich bieten wir Ihnen MARCKS Kits (22) und MARCKS Proteine (7) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 241 products:
Chinese Hamster Polyclonal MARCKS Primary Antibody für 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. in Journal of lipid research 2007
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Human Polyclonal MARCKS Primary Antibody für IHC - ABIN966536
Pariser, Herradon, Ezquerra, Perez-Pinera, Deuel: Pleiotrophin regulates serine phosphorylation and the cellular distribution of beta-adducin through activation of protein kinase C. in Proceedings of the National Academy of Sciences of the United States of America 2005
Human Polyclonal MARCKS Primary Antibody für 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. in The Journal of biological chemistry 2010
Show all 5 Pubmed References
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 (zeige SCNN1A Antikörper) activity is regulated by calpain-2 (zeige CAPN2 Antikörper) proteolysis of MARCKS.
In the absence of Pin1 (zeige PIN1 Antikörper), MARCKS is hyper-phosphorylated, leading to loss of cell adhesions, and collapse of the growth cone.
Findings suggest that MIR429 modulates mucin (zeige SLC13A2 Antikörper) 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 (zeige UHMK1 Antikörper) expression. Decreased KIS (zeige UHMK1 Antikörper) expression resulted in nuclear trapping of p27kip1 (zeige CDKN1B Antikörper) in VSMCs.
MARCKS regulates the expression of proinflammatory cytokines in macrophages through activation of p38 (zeige CRK Antikörper)/JNK (zeige MAPK8 Antikörper) MAPK (zeige MAPK1 Antikörper) and NF-kappaB (zeige NFKB1 Antikörper).
Targeting phospho-MARCKS overcomes drug-resistance and induces antitumor activity in preclinical models of multiple myeloma.
Grin 1 (zeige GPRIN1 Antikörper) is identified as a novel Cdk5 (zeige CDK5 Antikörper) substrate and MARCKS is confirmed as a Cdk5 (zeige CDK5 Antikörper) 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.
Authors determined that myristoylated alanine-rich C-kinase substrate (MARCKS) was highly expressed in ovarian stroma, and was required for the differentiation and tumor promoting function of CAFs (zeige TBX1 Antikörper).
Data indicate MARCKS (myristoylated alanine-rich C-kinase substrate) as a target of miR (zeige MLXIP Antikörper)-21.
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 (zeige CDC42 Antikörper), promoting neointima formation.
A novel role for MARCKS in regulating nuclear functions such as gene expression.
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 (zeige PKC Antikörper) mediated inhibition of endothelial L-arginine (zeige GATM Antikörper) 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)