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SVIL encodes a bipartite protein with distinct amino- and carboxy-terminal domains. Zusätzlich bieten wir Ihnen Supervillin Antikörper (37) und Supervillin Kits (4) und viele weitere Produktgruppen zu diesem Protein an.
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SVIL regulates neuronal maturation by controlling LSD1 (zeige KDM1A Proteine)+8a mediated histone H3K9 demethylation.
These results position archvillin as a mechanically sensitive component of the dystrophin (zeige DMD Proteine) complex and demonstrate that signaling defects caused by loss of gamma-SG (zeige SGCG Proteine) 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 (zeige ANLN Proteine) 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 (zeige TP53 Proteine) 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 (zeige KIR2DL1 Proteine) 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 (zeige AR Proteine) and modulates its transcriptional activity.
supervillin, an F-actin cross-linking protein (zeige ACTN2 Proteine), 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