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| Size | 100ug, 1MG |
|---|---|
| Isotype | IgG1, kappa |
| Brand | ProteoGenix |
| Product type | Primary Antibodies |
| Clonality | Monoclonal Antibody |
| Expression system | Mammalian cells |
| Applications | Elisa, WB |
| Product name | Gedivumab Biosimilar - Anti-hemagglutinin HA mAb - Research Grade |
|---|---|
| Source | CAS 1807954-17-1 |
| Species | Homo sapiens |
| Expression system | Mammalian cells |
| Purity | >85% |
| Buffer | PBS buffer PH7.5 |
| Delivery condition | Blue ice (+4°C) |
| Delivery Time | 3-5 days if in stock; 3-5 weeks if production needed |
| Storage condition | store at -80°C |
| Brand | ProteoGenix |
| Aliases /Synonyms | Gedivumab,MHAA4549A,RO6876802;RG7745,hemagglutinin HA,anti-hemagglutinin HA |
| Reference | PX-TA1463 |
| Note | For research use only. Not suitable for clinical or therapeutic use. |
| Isotype | IgG1-kappa |
| Clonality | Monoclonal Antibody |
Introduction to Gedivumab Biosimilar – A Promising Anti-hemagglutinin HA mAb for Therapeutic Targeting Gedivumab Biosimilar, also known as anti-hemagglutinin HA mAb, is a novel monoclonal antibody (mAb) that has shown great potential in the field of therapeutic targeting. This biosimilar is a highly specific and potent antibody that targets the hemagglutinin (HA) protein, which is a key component of the influenza virus. In this article, we will discuss the structure, activity, and potential applications of Gedivumab Biosimilar in detail.
Gedivumab Biosimilar is a recombinant humanized IgG1 monoclonal antibody that is produced using advanced genetic engineering techniques. It has a molecular weight of approximately 150 kDa and consists of two heavy chains and two light chains. The heavy chains are composed of four constant domains (CH1, CH2, CH3, and CH4) and one variable domain (VH), while the light chains contain two constant domains (CL) and one variable domain (VL). The variable domains of Gedivumab Biosimilar are responsible for its high specificity and binding affinity towards HA protein.
Gedivumab Biosimilar exerts its activity by specifically binding to the HA protein of the influenza virus. The HA protein is responsible for the attachment of the virus to the host cells and plays a crucial role in the viral entry and infection process. By binding to the HA protein, Gedivumab Biosimilar prevents the virus from attaching to the host cells, thereby inhibiting its entry and replication. This antibody also activates the body’s immune response, leading to the destruction of the virus and infected cells.
Gedivumab Biosimilar has shown promising results in preclinical studies and is currently being evaluated for its potential therapeutic applications. It has been found to be effective against a wide range of influenza virus strains, including the highly pathogenic H5N1 and H1N1 strains. This makes it a potential candidate for the prevention and treatment of influenza infections. Moreover, Gedivumab Biosimilar has also shown potential in reducing the severity of symptoms and improving the survival rate in animal models of influenza infection.
Apart from its use in influenza, Gedivumab Biosimilar is also being investigated for its potential in other viral infections, such as respiratory syncytial virus (RSV) and coronavirus. The HA protein of these viruses shares structural similarities with the influenza virus, making Gedivumab Biosimilar a potential therapeutic option for these infections as well.
In addition to its therapeutic applications, Gedivumab Biosimilar is also being studied for its potential use in diagnostic and research purposes. Its high specificity and binding affinity towards HA protein make it a valuable tool for the detection and quantification of influenza virus in clinical and research settings.
In summary, Gedivumab Biosimilar is a promising anti-hemagglutinin HA mAb that has shown great potential in the field of therapeutic targeting. Its unique structure and mechanism of action make it a highly specific and potent antibody against the influenza virus. With ongoing research and clinical trials, Gedivumab Biosimilar has the potential to become a valuable addition to the arsenal of treatments for influenza and other viral infections.
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