Recombinant Human Septin-2 (SEPT2) Protein (His-SUMO)

Name: Recombinant Human Septin-2 (SEPT2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09327P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Septin-2 (SEPT2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q15019
Target Symbol	SEPT2
Synonyms	SEPTIN2; DIFF6; KIAA0158; NEDD5; SEPT2; Septin-2; Neural precursor cell expressed developmentally down-regulated protein 5; NEDD-5
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHNIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDGDGGALGHHV
Expression Range	1-361aa
Protein Length	Full Length
Mol. Weight	57.5kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Cleavage furrow. Midbody. Cytoplasm, cell cortex. Cell projection, cilium membrane. Cell projection, cilium, flagellum.
Protein Families	TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
Database References	HGNC: 7729 OMIM: 601506 KEGG: hsa:4735 STRING: 9606.ENSP00000353157 UniGene: Hs.721234
Tissue Specificity	Widely expressed. Up-regulated in liver cancer.

Gene Functions References

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
Study discloses both SEPT2 and SEPT7 are essential for breast cancer cell migration and invasion by controlling MEK/ERK MAPKs activation. PMID: 27557506
Depletion of septin 2 reduces Drp1 recruitment to mitochondria and results in hyperfused mitochondria and delayed FCCP-induced fission. PMID: 27215606
septins protect ErbB2 from ubiquitylation, endocytosis and lysosomal degradation. Septin oligomerization regulates persistent expression of ErbB2/HER2 in gastric cancer cells. PMID: 27048593
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
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
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
Data indicate that forchlorfenuron (FCF) exhibits differential binding preference for septins SEPT2 and SEPT3. PMID: 24787956
Authors report here that the septins SEPT2, -9, -11, and probably -7 form fibrillar structures around the chlamydial inclusion. PMID: 25293760
Suggest PPAR-gamma activation down-regulates hepatocellular carcinoma cell SEPT2 levels to prevent tumor growth. PMID: 25592041
SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9. PMID: 23572511
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
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
The SEPT2 provides the directional guidance cues necessary for polarizing the epithelial microtubule network. PMID: 21788367
septin-2 plays a fundamental role in regulating barrier function by altering cortical actin expression. PMID: 20870893
the role of SEPT2 and SEPT11 in the InlB-Met interactions PMID: 21504731
Data show that Septins of the SEPT6 group preferentially interacted with septins of the SEPT2 group, SEPT3 group and SEPT7 group. PMID: 21082023
Nedd5 is involved in the process of cytokinesis in human brain tumours. PMID: 12125979
septins may form a mitotic scaffold for CENP-E and other effectors to coordinate cytokinesis with chromosome congression and segregation PMID: 15774761
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
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
septin 2, 6, and 7 complexes make up polymerized filaments PMID: 16914550
crystal structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex PMID: 17637674
Study shows that in epithelial cells septin 2 fibers colocalize with a subset of microtubule tracks composed of polyglutamylated tubulin. PMID: 18209106
A novel MLL-SEPT2 fusion variant in therapy-related myelodysplastic syndrome is reported. PMID: 18656699
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
SEPT2 is essential for the InlB-mediated entry of Listeria, but SEPT11 is not, which distinguishes the roles of different mammalian septins PMID: 19234302

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.