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SVIL encodes a bipartite protein with distinct amino- and carboxy-terminal domains. Additionally we are shipping Supervillin Antibodies (37) and Supervillin Kits (4) and many more products for this protein.
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SVIL regulates neuronal maturation by controlling LSD1 (show KDM1A Proteins)+8a mediated histone H3K9 demethylation.
These results position archvillin as a mechanically sensitive component of the dystrophin (show DMD Proteins) complex and demonstrate that signaling defects caused by loss of gamma-SG (show SGCG Proteins) occur both at the sarcolemma and in the nucleus.
Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin (show ANLN Proteins) additively increases cell division failure.
An actin/myosin-II-binding protein, supervillin (SVIL), is a substrate of PLK1.
adhesion regulatory protein supervillin increases cell survival by decreasing levels of the tumor suppressor protein p53 (show TP53 Proteins) and downstream target genes
Human genome-wide association and mouse knockout approaches identify platelet supervillin as an inhibitor of thrombus formation under shear stress.
supervillin is a novel molecule that associates with KIR2DL1 (show KIR2DL1 Proteins) receptor and regulates the inhibitory signaling in NK cells.
Supervillin, like its interactors, is important for efficient cytokinesis.
supervillin, F-actin and associated proteins coordinate a rapid, basolateral membrane recycling pathway that contributes to ERK signaling and actin-based cell motility
Supervillin associates with androgen receptor (show AR Proteins) and modulates its transcriptional activity.
supervillin, an F-actin cross-linking protein (show ACTN2 Proteins), localizes to cuticular plates in hair cells of the mouse cochlea and vestibule. Supervillin localizes near the apicolateral margins within the head plates of Deiters' cells and outer pillar cells, and proximal to the apicolateral margins of inner phalangeal cells. Overall, supervillin localization suggests this protein may shape the surface structure of the organ of Corti.
archvillin is among the first costameric proteins to assemble during myogenesis and that it contributes to myogenic membrane structure and differentiation.
supervillin (SV)--a peripheral membrane protein that binds myosin II and F-actin in such cells--negatively regulates stress fibers, focal adhesions, and cell-substrate adhesion
This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. The encoded protein appears to aid in both myosin II assembly during cell spreading and disassembly of focal adhesions. Two transcript variants encoding different isoforms of supervillin have been described.
, membrane-associated F-actin binding protein p205
, supervillin muscle-specific isoform