Recombinant Human SEPT7/SEPTIN7 Protein

Beta LifeScience SKU/CAT #: BLA-0005P

Recombinant Human SEPT7/SEPTIN7 Protein

Beta LifeScience SKU/CAT #: BLA-0005P
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Product Overview

Host Species Human
Accession Q16181
Synonym CDC10 CDC10 protein homolog CDC3 Cell division cycle 10 NBLA02942 SEPT7 SEPT7_HUMAN SEPT7A Septin 7 Septin-7
Description Recombinant Human SEPT7/SEPTIN7 Protein was expressed in Wheat germ. It is a Full length protein
Source Wheat germ
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped on dry ice. Upon delivery aliquot and store at -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. 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.
Subcellular Location Cytoplasm. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Midbody. Cytoplasm, cytoskeleton, cilium axoneme. Cell projection, cilium, flagellum.
Protein Families TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
Database References
Tissue Specificity Widely expressed.

Gene Functions References

  1. The present study identified that SEPT7 was a potential target of miR5903p and demonstrated that SEPT7 is associated with mediating the proapoptotic effect of miR5903p in human osteoblast cell line hFOB 1.19. PMID: 29568931
  2. SEPT7 overexpression and knockdown sept7 protein suppress the expression of 78 kDa glucoseregulated protein (GRP78), C/EBPhomologous protein (CHOP), pro-caspase3 and cleaved caspase3 and eIf 2alpha protein. PMID: 29344665
  3. Study discloses both SEPT2 and SEPT7 are essential for breast cancer cell migration and invasion by controlling MEK/ERK MAPKs activation. PMID: 27557506
  4. SUMOylation of human septins is critical for septin filament bundling and cytokinesis. PMID: 29051266
  5. Low SEPT7 expression is associated with glioma cell invasion. PMID: 27006177
  6. The results of this study found that bipolar Neural crest cells progenitors lose their polarity, retracting their processes to round for division, but generate neurons with bipolar morphology by emitting processes from the same locations as the progenitor. PMID: 28817802
  7. Results show that SEPT7 is involved in glioma cell migration with the assistance of cofilin phosphomediated cytoskeleton locomotion. PMID: 26846171
  8. Septin6 and Septin7 GTP binding proteins regulate AP-3- and ESCRT-dependent multivesicular body biogenesis PMID: 25380047
  9. Significantly lower SEPT7 expression in all expressional categories in encapsulated papillary thyroid carcinoma, follicular variant group may be a sign of different molecular signature in this type of tissue. PMID: 24685401
  10. In response to Candida albicans infection, SEPT7 forms a complex with endothelial cell N-cadherin, is required for normal accumulation of N-cadherin around hyphae, and is necessary for maximal fungal endocytosis. PMID: 24345743
  11. Significantly lower SEPT7 expression in encapsulated follicular variant of papillary thyroid carcinoma may be a sign of different molecular signature in this type of tissue. PMID: 24685401
  12. SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9. PMID: 23572511
  13. miR-30a-5p is a bona fide negative regulator of SEPT7 and the oncogenic activity of miR-30a-5p in human gliomas is at least in part through the repression of SEPT7 PMID: 23383034
  14. Myeloid K562 cells express three SEPT9 isoforms, all of which have an equal propensity to hetero-oligomerize with SEPT7-containing hexamers to generate octameric heteromers. PMID: 22956766
  15. Mutagenic analyses revealed that mutation of a potential phosphorylation site in SEPT7 (Y318) regulates the interaction with other septins. PMID: 21767235
  16. the purification, crystallization and structure for the GTP-binding domain of human septin 7 PMID: 22064074
  17. Sept7 occupies the ends of hexameric building blocks which assemble into non-polarised filaments. PMID: 21824007
  18. The SEPT7 provides the directional guidance cues necessary for polarizing the epithelial microtubule network. PMID: 21788367
  19. Data show that Septins of the SEPT6 group preferentially interacted with septins of the SEPT2 group, SEPT3 group and SEPT7 group. PMID: 21082023
  20. SEPT7 gene expression is decreased in follicular variant of papillary thyroid carcinoma. PMID: 21509594
  21. SEPT7 is involved in the regulation of sperm maturation. PMID: 20352323
  22. The expression of SEPT7 mRNA was significantly decreased by 6.9% in subjects with schizophrenia. PMID: 20385374
  23. This study demonstrates that SEPT7 is involved in gliomagenesis and suppresses glioma cell growth. PMID: 20035367
  24. SEPT7 plays an important role in the glioma cell invasion. PMID: 19916744
  25. regulated but the expression of CDK9, CDC20 and CLK3 was down- regulated in azoospermic testes. PMID: 19426592
  26. Sept7/9b/11 form a complex that has effects on filament elongation, bundling, or disruption PMID: 15485874
  27. septin 2, 6, and 7 complexes make up polymerized filaments PMID: 16914550
  28. crystal structures of the human SEPT2 G domain and the heterotrimeric human SEPT2-SEPT6-SEPT7 complex PMID: 17637674
  29. Demonstrate connection between septins/SOCS7/NCK signaling and the DNA damage response. PMID: 17803907
  30. SEPT7 forms a link between kinetochore distribution of CENP-E and the mitotic spindle checkpoint. PMID: 18460473
  31. SEPT7 gene can inhibit the invasion and migration ability of U251 glioma cells by reversing imbalanced state of MMPs/TIMPs, downregulating expression of integrin alpha(v)beta(3) and altering structure of tubulin-alpha. PMID: 18543212


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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.

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