Human Septin-2(SEPT2) ELISA kit

Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation. 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: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.

1. Results demonstrate that in stored platelets, septine-2 and septin-6 mRNAs have miR- 223 target sites, septin-2 and septin-6 are in complex with Ago-2. The results demonstrate that like in nucleated cells, enucleated platelets also have microRNA-based mechanisms for the regulation of their septins. PMID: 29943706
2. Study discloses both SEPT2 and SEPT7 are essential for breast cancer cell migration and invasion by controlling MEK/ERK MAPKs activation. PMID: 27557506
3. Depletion of septin 2 reduces Drp1 recruitment to mitochondria and results in hyperfused mitochondria and delayed FCCP-induced fission. PMID: 27215606
4. septins protect ErbB2 from ubiquitylation, endocytosis and lysosomal degradation. Septin oligomerization regulates persistent expression of ErbB2/HER2 in gastric cancer cells. PMID: 27048593
5. 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-140-5p. PMID: 27155525
6. 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 PMID: 26780475
7. These results suggest that SEPTIN2-mediated cytoskeletal rearrangement and STATHMIN-mediated differentiation may contribute to changes in cell morphology and differentiation of H/RS cells with CD99 upregulation in Hodgkin lymphoma. PMID: 26000982
8. Data indicate that forchlorfenuron (FCF) exhibits differential binding preference for septins SEPT2 and SEPT3. PMID: 24787956
9. s report here that the septins SEPT2, -9, -11, and probably -7 form fibrillar structures around the chlamydial inclusion. PMID: 25293760
10. Suggest PPAR-gamma activation down-regulates hepatocellular carcinoma cell SEPT2 levels to prevent tumor growth. PMID: 25592041
11. SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9. PMID: 23572511
12. The results shown in study support the hypothesis that single Septin 2, when present in excess or with unbalanced stoichiometries, may be unstable and assemble into amyloid-like structures. PMID: 21967827
13. Data illustrated roles of SEPT9 that might contribute to hetero-trimeric septin complex formation. SEPT9 can substitute for septins of the SEPT2 group and partially for SEPT7. PMID: 21767235
14. The SEPT2 provides the directional guidance cues necessary for polarizing the epithelial microtubule network. PMID: 21788367
15. septin-2 plays a fundamental role in regulating barrier function by altering cortical actin expression. PMID: 20870893
16. the role of SEPT2 and SEPT11 in the InlB-Met interactions PMID: 21504731
17. Data show that Septins of the SEPT6 group preferentially interacted with septins of the SEPT2 group, SEPT3 group and SEPT7 group. PMID: 21082023
18. Nedd5 is involved in the process of cytokinesis in human brain tumours. PMID: 12125979
19. septins may form a mitotic scaffold for CENP-E and other effectors to coordinate cytokinesis with chromosome congression and segregation PMID: 15774761
20. Nedd5 C-terminal is a novel autoantigen in systemic lupus erythematosus (SLE) patients and may be a valuable tool for diagnosing neuropsychiatric SLE. PMID: 15987492
21. protein encoded by SEPT2 is highly homologous to septins 1, 4 and 5 and is involved in the coordination of several key steps of mitosis PMID: 16682951
22. septin 2, 6, and 7 complexes make up polymerized filaments PMID: 16914550
23. crystal structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex PMID: 17637674
24. Study shows that in epithelial cells septin 2 fibers colocalize with a subset of microtubule tracks composed of polyglutamylated tubulin. PMID: 18209106
25. A novel MLL-SEPT2 fusion variant in therapy-related myelodysplastic syndrome is reported. PMID: 18656699
26. confirmed that the phosphorylation of SEPT2 on Ser218 by CK2 was crucial to the proliferation of HCC. These results suggest that SEPT2 might be a promising target for liver cancer therapy PMID: 19165576
27. SEPT2 is essential for the InlB-mediated entry of Listeria, but SEPT11 is not, which distinguishes the roles of different mammalian septins PMID: 19234302

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Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Cytoplasm, cell cortex. Cell projection, cilium membrane. Cell projection, cilium, flagellum.

TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family

Widely expressed. Up-regulated in liver cancer.

HGNC: 7729

OMIM: 601506

KEGG: hsa:4735

STRING: 9606.ENSP00000353157

UniGene: Hs.721234