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Filament-forming cytoskeletal GTPase. Additionally we are shipping Septin 2 Antibodies (110) and Septin 2 Kits (1) and many more products for this protein.
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Depletion of septin 2 reduces Drp1 recruitment to mitochondria and results in hyperfused mitochondria and delayed FCCP-induced fission.
septins protect ErbB2 (show ERBB2 Proteins) from ubiquitylation, endocytosis and lysosomal degradation. Septin (show SEPT6 Proteins) oligomerization regulates persistent expression of ErbB2/HER2 (show ERBB2 Proteins) in gastric cancer cells.
The results showed that SEPT2 has an oncogenic function through accelerated cell proliferation and invasion in biliary tract cancers, and is negatively regulated by miR (show MLXIP Proteins)-140-5p.
From the nucleotide-free structure some interesting conclusions about the nucleotide binding properties of Cdc11 can be drawn; especially when aligning the structure with the structure of GDP bound Sept2
These results suggest that SEPTIN2-mediated cytoskeletal rearrangement and STATHMIN (show STMN1 Proteins)-mediated differentiation may contribute to changes in cell morphology and differentiation of H/RS cells with CD99 (show CD99 Proteins) upregulation in Hodgkin lymphoma.
Data indicate that forchlorfenuron (FCF) exhibits differential binding preference for septins SEPT2 and SEPT3 (show SEPT3 Proteins).
Authors report here that the septins SEPT2, -9, -11, and probably -7 form fibrillar structures around the chlamydial inclusion.
Suggest PPAR-gamma (show PPARG Proteins) activation down-regulates hepatocellular carcinoma cell SEPT2 levels to prevent tumor growth.
SEPT2 forms a 1:1:1 complex with SEPT7 (show SEPT7 Proteins) and SEPT9 (show SEPT9 Proteins).
The results shown in study support the hypothesis that single Septin 2, when present in excess (show RCC1 Proteins) or with unbalanced stoichiometries, may be unstable and assemble into amyloid-like structures.
Results indicate a stimulatory role of septin-2 and the dynamic reorganization of septin (show SEPT6 Proteins) oligomers in exocytosis.
findings show SEPT2 is part of a diffusion barrier at the base of the ciliary membrane and is essential for retaining receptor-signaling pathways in the primary cilium
Further analysis based on antibody staining of central and peripheral nerves revealed beta-adducin (show ADD2 Proteins), septin 2, and sh3p8 (show SH3GL1 Proteins) as putative paranodal proteins.
Significant level of SEPT2 expression was found in heart in a developmentally regulated fashion.
p85 (show ECM1 Proteins) is thus involved in the spatial control of cytosolic division through regulation of Cdc42 (show CDC42 Proteins) and septin 2, in a PI3K-activity independent manner.
study identified control of septin (show SEPT6 Proteins) localization by the planar cell polarity (PCP (show PRCP Proteins)) protein Fritz (show WDPCP Proteins) as a crucial control point for both collective cell movement and ciliogenesis in embryos
Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes (By similarity).
, septin 2
, neural precursor cell expressed developmentally down-regulated protein 5
, neural precursor cell expressed, developmentally down-regulated 5
, neural precursor cell expressed, developmentally down-regulated gene 5
, vascular endothelial cell specific protein 11
, septin A