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Required for cytokinesis. Additionally we are shipping Anillin Antibodies (76) and Anillin Proteins (4) and many more products for this protein.
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Knockdown of ANLN in liver cells blocks cytokinesis and inhibits development of liver tumors.
Authors found that decreasing Ran-GTP (show AK3 ELISA Kits) levels or tethering active Ran to the equatorial membrane affects anillin's localization and causes cytokinesis phenotypes.
Anillin (ANLN) expression in tumor cells is correlated to poor prognosis in breast cancer patients, independent of Ki-67 (show MKI67 ELISA Kits) or tumor size.
ANLN expression is elevated in colorectal cancer and has a strong potential to act as a biomarker for the prognosis of colorectal cancer.
Findings indicate that miR (show MLXIP ELISA Kits)-497 is a potent tumor suppressor that inhibits cancer phenotypes by targeting ANLN and HSPA4L (show HSPA4L ELISA Kits) in NPC (show NPC1 ELISA Kits).
High nuclear expression of anillin (ANLN) is an independent predictor of poor disease-specific survival and it is a useful prognostic marker of urothelial carcinoma of the upper urinary tract (UCUT).
Data suggest that anillin (ANLN) could be involved in breast cancer progression and a potential target candidate in breast cancer.
Identification 4 novel and 18 known exonic ANLN variants associated with carotid intima-media thickness at bifurcation.
Anillin regulates intercellular adhesion in model human epithelia by mechanisms involving the suppression of JNK (show MAPK8 ELISA Kits) activity and controlling the assembly of the perijunctional cytoskeleton.
The sequestration of anillin by astral microtubules might alter the organization of cortical proteins to polarize cells for cytokinesis
Loss of ANLN expression is associated with tumorigenesis in liver.
data suggest that anillin is an essential intracellular component that maintains the integrity of asymmetric division in mouse oocytes.
Anillin is excluded from the cortex of first polar body, enriched in the cytokinetic ring that severs the polar body from the oocyte. In meiosis II, anillin is enriched in a cortical stripe coincident with and overlying the meiotic spindle midzone.
Results show that targeting of mDia2 to the cleavage furrow requires not only its binding to RhoA but also its diaphanous-inhibitory domain, and identify anillin as a novel mDia2 interaction partner.
we show that the transition from the actomyosin contractile ring to the midbody ring proceeds via a previously uncharacterized maturation process that requires opposing mechanisms of removal and retention of the scaffold protein (show HOMER1 ELISA Kits) Anillin.
Anillin is required for complete closure of the contractile ring and formation of the midbody ring during cytokinesis.
the anillin pleckstrin homology domain has two functions: targeting anillin to the plasma membrane furrow by binding to phosphatidylinositol phosphate lipids to maintain furrow organization and recruiting septins to the furrow.
Data suggest that Cindr and Anillin cooperate to promote intercellular bridge stability during incomplete cytokinesis in Drosophila melanogaster.
Results show that the anillin-septin and cadherin-catenin complexes can serve as alternative cassettes to promote tight physical coupling of F-actin and myosin II to the cleavage furrow and successful completion of cytokinesis.
anillin has a role in spatially regulating the contractile activity of myosin II during cytokinesis
important role for scraps in scaffolding cleavage furrow components, directly stabilizing intracellular bridges
A novel RhoGEF(Pbl)-dependent input promotes the simultaneous association of anillin with the plasma membrane, septins, and microtubules, independently of F-actin.
anillin and Peanut are involved in pseudocleavage furrow ingression in syncytial embryos, a process that is regulated by Ran
The authors propose that anillin is required for proper Rho-GTP (show AK3 ELISA Kits) distribution at cell-cell junctions and for maintenance of a robust apical actomyosin belt, which is required for cell-cell junction integrity.
The study provides the in vivo evidence for the requirement of Anillin during asymmetric neurogenic divisions.
Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression (By similarity).
actin-binding protein anillin
, anillin, actin binding protein
, anillin, actin binding protein (scraps homolog, Drosophila)
, actin-binding protein anillin-like
, Actin-binding protein 8
, lethal (2) k08255
, contractile ring component anillin