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The protein encoded by MARCKS is a substrate for protein kinase C. Additionally we are shipping MARCKS Kits (20) and MARCKS Proteins (7) and many more products for this protein.
Showing 10 out of 233 products:
Human Polyclonal MARCKS Primary Antibody for EIA, WB - ABIN357762
Rauch, Ferguson, Prestwich, Cafiso: Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. in The Journal of biological chemistry 2002
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Human Monoclonal MARCKS Primary Antibody for IF, WB - ABIN2838585
Lin, Fang, Park, Crews, Adler: MARCKS and related chaperones bind to unconventional myosin V isoforms in airway epithelial cells. in American journal of respiratory cell and molecular biology 2010
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Human Polyclonal MARCKS Primary Antibody for WB - ABIN389097
Aderem: The MARCKS family of protein kinase-C substrates. in Biochemical Society transactions 1996
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Human Monoclonal MARCKS Primary Antibody for WB - ABIN393637
Techasen, Loilome, Namwat, Takahashi, Sugihara, Puapairoj, Miwa, Saya, Yongvanit: Myristoylated alanine-rich C kinase substrate phosphorylation promotes cholangiocarcinoma cell migration and metastasis via the protein kinase C-dependent pathway. in Cancer science 2010
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Human Polyclonal MARCKS Primary Antibody for IF, ELISA - ABIN1532929
Sakai, Hirai, Kudoh, Minoshima, Shimizu: Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C. in Genomics 1992
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Human Polyclonal MARCKS Primary Antibody for IF, WB - ABIN197064
Nagumo, Ikenoya, Sakurada, Furuya, Ikuhara, Hiraoka, Sasaki: Rho-associated kinase phosphorylates MARCKS in human neuronal cells. in Biochemical and biophysical research communications 2001
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Human Polyclonal MARCKS Primary Antibody for IF - ABIN401578
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
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Human Polyclonal MARCKS Primary Antibody for ELISA, WB - ABIN1531898
Mungall, Palmer, Sims, Edwards, Ashurst, Wilming, Jones, Horton, Hunt, Scott, Gilbert, Clamp, Bethel, Milne, Ainscough, Almeida, Ambrose, Andrews, Ashwell, Babbage, Bagguley, Bailey, Banerjee, Barker et al.: The DNA sequence and analysis of human chromosome 6. ... in Nature 2003
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 (show SCNN1A Antibodies) activity is regulated by calpain-2 (show CAPN2 Antibodies) proteolysis of MARCKS.
In the absence of Pin1 (show PIN1 Antibodies), MARCKS is hyper-phosphorylated, leading to loss of cell adhesions, and collapse of the growth cone.
Findings suggest that MIR429 modulates mucin (show SLC13A2 Antibodies) 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 (show UHMK1 Antibodies) expression. Decreased KIS (show UHMK1 Antibodies) expression resulted in nuclear trapping of p27kip1 (show CDKN1B Antibodies) in VSMCs.
MARCKS regulates the expression of proinflammatory cytokines in macrophages through activation of p38 (show CRK Antibodies)/JNK (show MAPK8 Antibodies) MAPK (show MAPK1 Antibodies) and NF-kappaB (show NFKB1 Antibodies).
Targeting phospho-MARCKS overcomes drug-resistance and induces antitumor activity in preclinical models of multiple myeloma.
Grin 1 (show GPRIN1 Antibodies) is identified as a novel Cdk5 (show CDK5 Antibodies) substrate and MARCKS is confirmed as a Cdk5 (show CDK5 Antibodies) 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 (show CALM1 Antibodies)) stimulates phosphoinositide-3-kinase (PI3K (show PIK3CA Antibodies)) lipid kinase activity by binding MARCKS and displacing it from phosphatidylinositol 4,5-bisphosphate (PIP2) headgroups, thereby releasing free PIP2 that recruits active PI3K (show PIK3CA Antibodies) 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 (show CDC42 Antibodies), 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 (show PKC Antibodies) mediated inhibition of endothelial L-arginine (show GATM Antibodies) 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)