Recombinant Human Septin-7 (SEPT7) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10443P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) SEPT7.

Recombinant Human Septin-7 (SEPT7) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-10443P
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Product Overview

Description Recombinant Human Septin-7 (SEPT7) 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 Q16181
Target Symbol SEPT7
Synonyms CDC10; CDC10 protein homolog; CDC3; Cell division cycle 10; NBLA02942; SEPT7; SEPT7_HUMAN; SEPT7A; Septin 7; Septin-7
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence SVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
Expression Range 2-437aa
Protein Length Full Length of Mature Protein
Mol. Weight 66.5kDa
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. 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

HGNC: 1717

OMIM: 603151

KEGG: hsa:989

STRING: 9606.ENSP00000381992

UniGene: PMID: 29568931

  • 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
  • Study discloses both SEPT2 and SEPT7 are essential for breast cancer cell migration and invasion by controlling MEK/ERK MAPKs activation. PMID: 27557506
  • SUMOylation of human septins is critical for septin filament bundling and cytokinesis. PMID: 29051266
  • Low SEPT7 expression is associated with glioma cell invasion. PMID: 27006177
  • 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
  • Results show that SEPT7 is involved in glioma cell migration with the assistance of cofilin phosphomediated cytoskeleton locomotion. PMID: 26846171
  • Septin6 and Septin7 GTP binding proteins regulate AP-3- and ESCRT-dependent multivesicular body biogenesis PMID: 25380047
  • 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
  • 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
  • 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
  • SEPT2 forms a 1:1:1 complex with SEPT7 and SEPT9. PMID: 23572511
  • 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
  • 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
  • Mutagenic analyses revealed that mutation of a potential phosphorylation site in SEPT7 (Y318) regulates the interaction with other septins. PMID: 21767235
  • the purification, crystallization and structure for the GTP-binding domain of human septin 7 PMID: 22064074
  • Sept7 occupies the ends of hexameric building blocks which assemble into non-polarised filaments. PMID: 21824007
  • The SEPT7 provides the directional guidance cues necessary for polarizing the epithelial microtubule network. PMID: 21788367
  • Data show that Septins of the SEPT6 group preferentially interacted with septins of the SEPT2 group, SEPT3 group and SEPT7 group. PMID: 21082023
  • SEPT7 gene expression is decreased in follicular variant of papillary thyroid carcinoma. PMID: 21509594
  • SEPT7 is involved in the regulation of sperm maturation. PMID: 20352323
  • The expression of SEPT7 mRNA was significantly decreased by 6.9% in subjects with schizophrenia. PMID: 20385374
  • This study demonstrates that SEPT7 is involved in gliomagenesis and suppresses glioma cell growth. PMID: 20035367
  • SEPT7 plays an important role in the glioma cell invasion. PMID: 19916744
  • regulated but the expression of CDK9, CDC20 and CLK3 was down- regulated in azoospermic testes. PMID: 19426592
  • Sept7/9b/11 form a complex that has effects on filament elongation, bundling, or disruption PMID: 15485874
  • 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
  • Demonstrate connection between septins/SOCS7/NCK signaling and the DNA damage response. PMID: 17803907
  • SEPT7 forms a link between kinetochore distribution of CENP-E and the mitotic spindle checkpoint. PMID: 18460473
  • 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

    • FAQs

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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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