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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Clostridium tetani tetX/Tetanus toxin/TeNT Protein, N-His |
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Origin species | Clostridium tetani (strain Massachusetts / E88) |
Expression system | Prokaryotic expression |
Molecular weight | 54.66 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 | Met1-Ser458 |
Aliases /Synonyms | Tetanus toxin, 3.4.24.68, Tentoxylysin, Tetanus toxin light chain, Tetanus toxin chain L, Tetanus toxin heavy chain, Tetanus toxin chain H, tetX, CTC_p60, Clostridium tetani (strain Massachusetts / E88) |
Reference | ARO-P10832 |
Note | For research use only. |
Recombinant Clostridium tetani tetX/Tetanus toxin/TeNT protein is a genetically engineered protein that is derived from the bacteria Clostridium tetani, the causative agent of tetanus. This protein is a potent neurotoxin that is responsible for the severe symptoms of tetanus, including muscle stiffness and spasms. The recombinant version of this protein has been extensively studied and has shown promising results in various applications, including vaccine development and therapeutic use.
The recombinant Clostridium tetani tetX/Tetanus toxin/TeNT protein is a large molecule with a molecular weight of approximately 150 kDa. It is composed of a heavy chain (Hc) and a light chain (Lc) that are connected by a disulfide bond. The heavy chain is responsible for binding to specific receptors on nerve cells, while the light chain is responsible for the toxin’s enzymatic activity.
The Hc of the recombinant protein is composed of two domains, the C-terminal domain (Hc-C) and the N-terminal domain (Hc-N). The Hc-C domain is responsible for binding to the neuronal membrane, while the Hc-N domain is involved in receptor binding and internalization. The Lc of the recombinant protein is composed of a single domain that possesses the enzymatic activity responsible for cleaving specific proteins involved in neurotransmission.
The recombinant Clostridium tetani tetX/Tetanus toxin/TeNT protein is a potent neurotoxin that acts by blocking the release of inhibitory neurotransmitters, such as glycine and GABA, from nerve cells. This results in uncontrolled muscle contractions and spasms, which are characteristic symptoms of tetanus. The enzymatic activity of the Lc of the protein is responsible for cleaving specific proteins involved in the release of these neurotransmitters, leading to their inhibition.
Besides its neurotoxic activity, the recombinant protein also has immunogenic properties. It can elicit a strong immune response in the host, leading to the production of antibodies against the toxin. This makes it an excellent candidate for vaccine development against tetanus.
Recombinant Clostridium tetani tetX/Tetanus toxin/TeNT protein has several applications, including vaccine development and therapeutic use.
The recombinant protein has been extensively studied as a potential vaccine candidate against tetanus. It has been shown to elicit a strong immune response in animal models, leading to the production of neutralizing antibodies against the toxin. This makes it a promising candidate for the development of a safe and effective vaccine against tetanus.
In addition, the recombinant protein can be used as a carrier protein for other antigens, making it a potential candidate for the development of multivalent vaccines against other diseases.
The recombinant protein has also shown potential for therapeutic use in the treatment of tetanus. It can be used as a passive immunotherapy, where the recombinant protein is administered to individuals who have already been exposed to the tetanus toxin. This can help neutralize the toxin and prevent its harmful effects.
In addition, the recombinant protein can be used as an adjuvant in cancer therapy. Studies have shown that the toxin can target and kill specific cancer cells, making it a potential candidate for targeted cancer therapy.
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