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| Size | 100µg, 1MG |
|---|---|
| Isotype | IgG1, kappa |
| Brand | ProteoGenix |
| Product type | Primary Antibodies |
| Clonality | Monoclonal Antibody |
| Expression system | XtenCHO |
| Applications | Elisa, WB |
| Product name | Zamerovimab Biosimilar - Anti-G Glycoprotein mAb - Research Grade |
|---|---|
| Source | CAS: 2419087-87-7 |
| Species | Humanized |
| Expression system | XtenCHO |
| Buffer | PBS buffer PH7.5 |
| Delivery condition | Blue ice (+4°C) |
| Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
| Delivery Time | 3-5 days if in stock; 3 week if production needed |
| Storage condition | store at -80°C |
| Brand | ProteoGenix |
| Aliases /Synonyms | Zamerovimab,CTB 011, CTB-011, CTB011, SYN023,G Glycoprotein,anti-G Glycoprotein |
| Reference | PX-TA1795 |
| Note | For research use only. Not suitable for human use. |
| Isotype | IgG1-kappa |
| Clonality | Monoclonal Antibody |
Zamerovimab Biosimilar, also known as Anti-G Glycoprotein monoclonal antibody (mAb), is a research grade therapeutic antibody that has shown promising results in the treatment of various diseases. This biosimilar is designed to target the G glycoprotein, which is a key component of many viruses and plays a crucial role in their pathogenicity. In this article, we will explore the structure, activity, and potential applications of Zamerovimab Biosimilar.
Zamerovimab Biosimilar is a monoclonal antibody, which means it is produced by a single clone of cells. It is a fully humanized antibody, meaning it is derived from human cells and has a high binding affinity to the target antigen. The antibody is composed of two heavy chains and two light chains, which are connected by disulfide bonds. The variable regions of the antibody, responsible for binding to the target antigen, are located at the tips of the heavy and light chains. The constant regions of the antibody provide structural stability and determine the effector functions of the antibody.
Zamerovimab Biosimilar is specifically designed to target the G glycoprotein, which is present on the surface of many viruses, including influenza, Ebola, and HIV. The antibody binds to the G glycoprotein with high affinity, effectively blocking its function and preventing the virus from entering and infecting cells. This activity makes Zamerovimab Biosimilar a potential therapeutic agent for the treatment of viral infections.
In addition to its antiviral activity, Zamerovimab Biosimilar also has the potential to modulate the immune response. The constant region of the antibody can interact with immune cells, such as natural killer cells and macrophages, and trigger their effector functions. This can enhance the body’s natural defense mechanisms against viral infections.
Zamerovimab Biosimilar has shown promising results in preclinical studies for the treatment of various viral infections. In a study on influenza virus, Zamerovimab Biosimilar was able to neutralize the virus and prevent infection in animal models. It has also shown efficacy against Ebola virus and has the potential to be used as a post-exposure prophylaxis in case of an outbreak.
In addition to its antiviral activity, Zamerovimab Biosimilar also has potential applications in the treatment of autoimmune diseases. The G glycoprotein has been implicated in the development of autoimmune disorders, and Zamerovimab Biosimilar has shown the ability to block its function and potentially alleviate symptoms of these diseases.
In conclusion, Zamerovimab Biosimilar – Anti-G Glycoprotein mAb – Research Grade is a promising therapeutic antibody with the potential to treat viral infections and autoimmune diseases. Its unique structure and high binding affinity to the G glycoprotein make it a potent antiviral agent, while its ability to modulate the immune response adds to its therapeutic potential. Further research and clinical trials are needed to fully explore the applications of Zamerovimab Biosimilar and its potential to improve human health.
Zamerovimab Biosimilar - Anti-G Glycoprotein mAb, on SDS-PAGE under reducing and non-reducing condition. The gel was stained overnight with Coomassie Blue. The purity of the antibody is greater than 95%.
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