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SEPT8 is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Additionally we are shipping Septin 8 Antibodies (61) and Septin 8 Kits (4) and many more products for this protein.
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Results show that sept8a is broadly expressed in the developing brain and the gill arches of larvae. Brains of adult zebrafish reveal a large spatial overlap of sept8a and sept8b expression with few regions uniquely expressing sept8a or sept8b.
SEPT8 modulates beta-amyloidogenic processing of APP (show APP Proteins) through a mechanism affecting the intracellular sorting and accumulation of BACE1 (show BACE Proteins).
Cloning, overexpression, purification and preliminary characterization of human septin 8. Fluorescence emission spectra, analytic gel filtration and DLS reflect the sample oligomeric heterogeneity with the predominance of dimers in solution.
SEPT8 and SEPT4 (show SEPT4 Proteins) are localized surrounding alpha-granules. Activation of platelets by agonists resulted in the translocation of SEPT4 (show SEPT4 Proteins) and SEPT8 to the platelet surface indicating a possible functional role of these proteins in platelet granular secretion
We studied the assembly of three human septins, SEPT4 (show SEPT4 Proteins), SEPT5 (show SEPT5 Proteins) and SEPT8, with each other (heterotypic) and with themselves (homotypic) using a yeast two-hybrid system.
Our finding suggests a role for members of the septin (show SEPT6 Proteins) family in the development of proliferative retinal membranes.
Signaling protein ras-related protein rab-7A (show RAB7A Proteins) and septin 8 levels were significantly higher in hippocampus of poor contextual fear conditioning extinguishers.
Septin 8 is present in specific location within retina. Disappearance of septin 8 in nuclei of photoreceptor cells is concomitant with nuclear DNA fragmentation.
This gene is a member of the septin family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse, and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells.
, septin 8, isoform 1