The septin family of nucleotide-binding proteins was originally identified in yeast as cell division regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse; they are thought to regulate cytoskeletal organization.
Septin 4 is encoded by the SEPT4 gene in humans and is expressed at high levels in the brain and heart. It is a filament-forming GTPase that is localized to the cytoskeleton. Septin 4 may also play a role in cytokinesis. Septin 4 exists as several isoforms, one of which is found in mitochondria and is implicated in apoptosis and cancer. Alternate names for septin 4 include apoptosis-related protein in the TGF-beta signaling pathway (ARTS), bradeion beta, brain protein H5, H5, MART, SEP4, cell division control-related protein 2, cerebral protein 7, CE5B3, CE5B3 beta, Peanut-like protein 2 (PNUTL2), hucep-7, hCDCREL-2, and septin-M.
Septin 7 is highly similar to yeast CDC10, Drosophila Diff 6, and mouse H5 protein. Each of these proteins contains a GTP-binding motif. It functions in gliomagenesis and in the suppression of glioma cell growth. It is required for the association of centromere-associated protein E with the kinetochore during mitosis. Alternative splicing results in multiple isoforms of septin 7. Abnormal expression patterns of some septins have been reported in human cancers and neurodegenerative diseases. Alternate names include cell division cycle 10 (CDC10) homolog (S. cerevisiae), CDC3, CDC10, SEPT7A, and NBLA02942.
Antibodies for Septin Detection
The anti-human septin antibody products are affinity-purified IgG antibodies that recognize human septin 4 and septin 7 protein. The antibodies were raised in rabbit using synthetic peptides and can be used for Western blot (WB) detection or immunohistochemical (IHC) detection of human septin 4 or septin 7.