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HPA018481

Sigma-Aldrich

Anti-SEPT2 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-Protein NEDD5, Anti-Septin-2

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human, mouse, rat
mouse, human, rat

enhanced validation

RNAi knockdown
Learn more about Antibody Enhanced Validation

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

WGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGH

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SEPT2(4735)

General description

The gene septin-2 (SEPT2) is mapped to human chromosome 2q37. It belongs to a conserved family of guanosine triphosphate binding proteins required for cell division. SEPT2 is present at the mid-body, the cleavage furrow and the central spindle of cells undergoing cytokinesis. In metaphase cells, SEPT2 is present within the microtubule spindle. SEPT2 is widely expressed with highest levels in brain tissues.

Immunogen

Septin-2 recombinant protein epitope signature tag (PrEST)

Application

Anti-SEPT2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.

Biochem/physiol Actions

At metaphase septin-2 (SEPT2) is crucial for maintaining CENP-E (Centromere-associated protein E) at kinetochores, required for chromosome congression. In anaphase, SEPT2 is needed for chromosome segregation and spindle elongation. SEPT2 forms a complex with SEPT7 and SEPT9. All three together are present along the length of the axoneme in the primary cilium of retinal pigmented epithelial cells. The complex is crucial for ciliogenesis. SEPT2 is recruited to the site of bacterial entry next to actin and is involved in bacterial invasion of Listeria and Shigella. SEPT2 is up-regulated in human hepatoma carcinoma cells (HCC). Casein kinase-2 mediated phosphorylation of SEPT2 is important for proliferation of HCC.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST72699

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Serge Mostowy et al.
PloS one, 4(1), e4196-e4196 (2009-01-16)
Septins are conserved GTPases that form filaments and are required in many organisms for several processes including cytokinesis. We previously identified SEPT9 associated with phagosomes containing latex beads coated with the Listeria surface protein InlB. Here, we investigated septin function
Rania Ghossoub et al.
Journal of cell science, 126(Pt 12), 2583-2594 (2013-04-11)
Septins are a large, evolutionarily conserved family of GTPases that form hetero-oligomers and interact with the actin-based cytoskeleton and microtubules. They are involved in scaffolding functions, and form diffusion barriers in budding yeast, the sperm flagellum and the base of
Elias T Spiliotis et al.
Science (New York, N.Y.), 307(5716), 1781-1785 (2005-03-19)
Coordination of cytokinesis with chromosome congression and segregation is critical for proper cell division, but the mechanism is unknown. Here, septins, a conserved family of polymerizing guanosine triphosphate-binding proteins, localized to the metaphase plate during mitosis. Septin depletion resulted in
Joanna Kim et al.
Arteriosclerosis, thrombosis, and vascular biology, 41(1), 346-359 (2020-11-06)
Septin 2 is localized at junctions in human microvascular endothelial monolayers. The junctional localization of septin 2 is necessary for organization of cell-cell adhesion proteins of endothelial cells. Approach and Results: Septin 2 was depleted at junctions by suppression of
N Cerveira et al.
Oncogene, 25(45), 6147-6152 (2006-05-10)
We have identified a new mixed lineage leukemia (MLL) gene fusion partner in a patient with treatment-related acute myeloid leukemia (AML) presenting a t(2;11)(q37;q23) as the only cytogenetic abnormality. Fluorescence in situ hybridization demonstrated a rearrangement of the MLL gene

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