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| Size | 100ug |
|---|---|
| Brand | Arovia |
| Product type | Recombinant Proteins |
| Product name | Recombinant Human SEPTIN6 Protein, N-His |
|---|---|
| Origin species | Human |
| Expression system | Prokaryotic expression |
| Molecular weight | 34.62 kDa |
| Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Form | Liquid |
| Delivery condition | Dry Ice |
| Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
| Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
| Brand | Arovia |
| Host species | Escherichia coli (E.coli) |
| Fragment Type | Gly24-Gly307 |
| Aliases /Synonyms | SEPTIN6, KIAA0128, SEPT6, SEP2, Septin-6 |
| Reference | ARO-P12294 |
| Note | For research use only. |
Introduction:
Recombinant proteins are proteins that are artificially produced by inserting the genetic material for a specific protein into a host organism, such as bacteria or yeast. These proteins have become essential tools in various fields of research, including biotechnology, medicine, and drug development. One such protein is Recombinant Human SEPTIN6 Protein, which has gained significant attention in recent years due to its unique structure and diverse functions.
Structure of Recombinant Human SEPTIN6 Protein:
SEPTIN6 is a member of the septin protein family, which plays a crucial role in cellular processes such as cell division, signaling, and membrane trafficking. The human SEPTIN6 gene is located on chromosome 22 and encodes a protein of 437 amino acids. The primary structure of SEPTIN6 consists of a conserved GTP-binding domain and a C-terminal coiled-coil domain. The GTP-binding domain is responsible for the protein’s ability to bind to guanine nucleotides, while the coiled-coil domain allows for protein-protein interactions.
Activity of Recombinant Human SEPTIN6 Protein:
SEPTIN6 is primarily found in the cytoplasm of cells, where it forms hetero-oligomeric complexes with other septin family members. These complexes are essential for the organization and stability of the cytoskeleton, which is crucial for maintaining cell shape and movement. SEPTIN6 has also been shown to play a role in cytokinesis, the process of cell division, by forming a ring-like structure at the site of cell cleavage. Furthermore, SEPTIN6 has been implicated in various cellular processes such as vesicle trafficking, membrane fusion, and cell signaling.
Application of Recombinant Human SEPTIN6 Protein:
Recombinant Human SEPTIN6 Protein has several potential applications in the field of biotechnology and medicine. One of its most significant uses is as an antigen for the production of antibodies. Antibodies against SEPTIN6 can be used in research to study the protein’s function and localization within cells. They can also be used in diagnostic tests for diseases where SEPTIN6 is overexpressed, such as certain types of cancer.
SEPTIN6 has also been identified as a potential therapeutic target in cancer treatment. Studies have shown that SEPTIN6 is overexpressed in several types of cancer, including breast, lung, and colon cancer. Inhibiting SEPTIN6 activity has been shown to reduce tumor growth and metastasis, making it a promising target for drug development.
Furthermore, SEPTIN6 has been linked to several neurological disorders, including Alzheimer’s disease and Parkinson’s disease. Recombinant Human SEPTIN6 Protein can be used in research to study its role in these diseases and potentially develop new treatments.
Conclusion:
In conclusion, Recombinant Human SEPTIN6 Protein is a versatile protein with a unique structure and diverse functions. Its ability to form complexes with other septin family members makes it essential for various cellular processes, including cell division and signaling. With its potential applications in antibody production, cancer treatment, and neurological research, SEPTIN6 is a valuable tool in the scientific community. Further studies on this protein’s structure and activity may lead to new insights and potential therapeutic strategies for various diseases.
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