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Human Monoclonal MYH9 Primary Antibody for IF, IHC (p) - ABIN518147
Betapudi, Gokulrangan, Chance, Egelhoff: A proteomic study of myosin II motor proteins during tumor cell migration. in Journal of molecular biology 2011
Show all 2 Pubmed References
Dog (Canine) Polyclonal MYH9 Primary Antibody for WB - ABIN2783216
Sabbir, Dillon, Mowat: Dlc1 interaction with non-muscle myosin heavy chain II-A (Myh9) and Rac1 activation. in Biology open 2016
Dog (Canine) Polyclonal MYH9 Primary Antibody for ICC, IF - ABIN153126
Klingner, Cherian, Fels, Diesinger, Aufschnaiter, Maghelli, Keil, Beck, Tolić-Nørrelykke, Bathe, Wedlich-Soldner: Isotropic actomyosin dynamics promote organization of the apical cell cortex in epithelial cells. in The Journal of cell biology 2014
The actomyosin network is influenced by NMHC IIA and regulated by the factor CrpF46, which is involved in the control of cell migration.
Non-muscle myosin IIA is post-translationally modified by interferon-stimulated gene 15 in breast cancer cells
This study reports four novel MYH9 mutations affecting the tail domain of NMMHC-IIA and responsible for MYH9-RD in four families. Two variants cause amino acid substitutions in the coiled-coil region of NMMHC-IIA, while the other two are a splicing variant and a single nucleotide deletion both resulting in frameshift alterations of the short non-helical tailpiece.
c.5521G>A (p.Glu1841Lys) mutation in the MYH9 gene probably underlies the MYH9-related disease in this pedigree
A germline de novo MYH9 mutation was identified in a newborn with congenital hemangioma.
Molecular modeling/simulation coupled with site-directed mutagenesis revealed that Asp(147) or Asn(169) of RIPK1 are key for ceramide binding and that Arg(258) or Leu(293) residues are involved in the nonmuscle myosin heavy chain II-A interaction, leading to ceramidosome formation and necroptosis.
variant of MYH9 gene is the cause of Fechtner syndrome
2 SNPs of MYH9, rs12107 in the 3'UTR and rs2269529 in the coding region, are associated with increased risk of NSOCs and their subphenotypes in a Chinese population. These variants may contribute to the onset of NSOCs by increasing the expression level of MYH9.
The overall purpose of this review is to point out that important progresses have been made in understanding the pathogenesis of ANKRD26-Related Thrombocytopenia and MYH9-Related Diseases and new therapeutic approaches have been proposed and tested.
Myosin IIa as a physiological regulator of endothelial von Willebrand factor secretion in stress-induced hemostasis and thrombosis.
Myosin IIA and IIB are essential for the formation of transverse arcs and ventral stress fibers, respectively. Furthermore, the study illustrated the roles of both isoforms in lamellar flattening and also raised the possibility that actin filaments in ventral stress fibers are in a stretched conformation.
These results indicate that nonmuscle myosin heavy chain-IIs interact with sodium channel alpha subunits subunits in an isoform-dependent manner and influence their functional properties.
In neutrophilic leucocytes from MYH9-related disease patients NMIIa inclusions are accompanied by increased lipid storage in droplets, suggesting that NMIIa dysfunction may contribute to lipid imbalance in man.
A missense mutation (c.1124C>T:p.S375F) was found in a congenital thrombocytopenia patient and his affected mother. It was associated with abnormal neutrophil NMMHC-IIA localization.
Our results suggest that MYH9 rs3752462 is significantly associated with an increased risk of diabetic kidney disease in Chinese Han individuals.
Results suggest that coupling between actin and microtubule cytoskeletons driven by Myosin II and KIF20A ensures the spatial coordination between RAB6-positive vesicles fission from Golgi/trans-Golgi network membranes and their exit along microtubules.
These results suggest that cytoplasmic multimolecular protein complexes containing myosin-9 and tropomyosin are involved in the regulation of cellular response to LYSOPHOSPHATIDIC ACID.
miR-647 functions as a tumor metastasis suppressor in gastric cancer by targeting SRF/MYH9 axis.
MYO18A has the potential to form a multiprotein complex that links the Golgi apparatus to F-actin, which regulates muscle integrity and function during early development
Report that PTCSC2 binds myosin-9 (MYH9). In a bidirectional promoter shared by FOXE1 and PTCSC2, MYH9 inhibits the promoter activity in both directions. This inhibition can be reversed by PTCSC2, which acts as a suppressor.
These results actually support that NMHC-IIA is involved in negative modulation of the host innate immune system, which provides a molecular basis for prevention and control of the sialylated RNA viruses and treatment of inflammatory diseases.
In conclusion, the MYH9 E1841K variant alters podocyte cytoskeletal structure and renders podocytes more susceptible to injury after a damaging stimulus.
the severe migration defects indicate an essential and fundamental role of Myh9 for neutrophil trafficking in innate immunity.
the key role of NMMHC IIA in oxygen glucose-deprived -stimulated mouse brain bEND.3 endothelial cells, is reported.
NMIIa and actin filaments concentrate around lipid droplets (LDs), and form transient foci between dissociating LDs. NMIIa depletion results in decreased LD dissociations, enlarged LDs, decreased hydrolysis and increased storage of triglycerides.
data therefore reveal a role for NMIIA and NMIIB as negative regulators of proliferation in the mammary epithelium.
Fluorescence resonance energy transfer experiments showed that FliI-NMMIIA interactions require Ca(2+) influx. We conclude that Ca(2+) influx through the TRPV4 channel regulates FliI-NMMIIA interaction, which in turn enables generation of the cell extensions essential for collagen remodeling
Collectively, these results implicate both moesin and myosin IIA in the regulation of phagolysosome biogenesis and in host defense against infections.
APPL1 enhances glucose uptake by modulating the activation and localization of PKCzeta, as well as its functional interaction with both PP2A and myosin IIa.
Data show that deletion of myosin heavy chain II-A (Myh9)/myosin heavy chain II-B (Myh10) caused severe hydroureter/hydronephrosis at birth.
our data indicated that PGDHC is a Pg-derived, cell-permeable ceramide that possesses a unique property of promoting osteoclastogenesis via interaction with Myh9 which, in turn, activates a Rac1/DC-STAMP pathway for upregulation of osteoclast cell fusion.
Conditional deletion of nonmuscle myosin II-A in mouse tongue epithelium results in squamous cell carcinoma
Inhibition of NMMHC IIA impedes TF expression and venous thrombosis via Akt/GSK3beta-NF-kappaB signalling pathways in the endothelium both in vitro and in vivo.
Myh9 mediates colitis-induced epithelium injury by restricting Lgr5+ stem cells
Mst1 regulates Myosin IIa dynamics to organize high and low affinity LFA-1 to the anterior and posterior membrane during T cell migration.
regulates morphogenesis of immature nephrons
DDR1 malfunction causes outer hair cells deformation and the separation of the lateral wall, the location of the cellular motor responsible for the electromotile property, explicitly in those regions showing DDR1 and NM-IIA co-localization.
A new role for Arl13b in actin cytoskeleton remodeling through the interaction with Myh9.
Lgl1 forms two distinct complexes in vivo, Lgl1-NMIIA and Lgl1-Par6alpha-aPKCzeta, and that the formation of these complexes is affected by the phosphorylation state of Lgl1.
The distribution of organelles within platelets critically depends on a homogeneous organelle distribution within megakaryocytes and preplatelet fragments, which requires myosin IIA.
Results demonstrate an important role of NMHC-IIA for the proper formation and function of the glomerulus in zebrafish.
Data show that the locomotion and blebbing of the primordial germ cells (PGCs) required F-actin, myosin II activity and RhoA/Rho-associated protein kinase (ROCK) signaling.
MYH9 physically interacts with the porcine reproductive and respiratory syndrome virus GP5 protein via its C-terminal domain and confers susceptibility of cells to virus infection.
This gene encodes a conventional non-muscle myosin\; this protein should not be confused with the unconventional myosin-9a or 9b (MYO9A or MYO9B). The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness.
cellular myosin heavy chain, type A
, myosin heavy chain 9
, myosin heavy chain, non-muscle IIa
, non-muscle myosin heavy chain A
, non-muscle myosin heavy chain IIa
, non-muscle myosin heavy polypeptide 9
, nonmuscle myosin heavy chain II-A
, myosin IIA
, myosin heavy chain IX
, myosin, heavy chain 9, non-muscle, like-2
, myosin, heavy polypeptide 9, non-muscle
, NMMHC II-a
, heavy polypeptide 9
, myosin heavy chain, nonmuscle
, non-muscle IIa
, type A
, nonmuscle myosin II heavy chain A