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| Size | 100ug, 1MG |
|---|---|
| Brand | ProteoGenix |
| Isotype | Ig single chain of 5 VH (sc-5-VH) |
| Product type | Primary Antibodies |
| Clonality | Monoclonal Antibody |
| Expression system | XtenCHO |
| Applications | Elisa |
| Product name | Lunsekimig Biosimilar - Anti-IL13; Albumin mAb - Research Grade |
|---|---|
| Source | CAS: 2770858-49-4 |
| Origin species | Humanized |
| Expression system | XtenCHO |
| Purity | >95% by SDS-PAGE. |
| Buffer | 0.01M PBS, pH 7.4. |
| Delivery condition | Blue ice (+4°C) |
| 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; -20°C for long term |
| Brand | ProteoGenix |
| Reference | PX-TA2126 |
| Note | For research use only. Not suitable for human use. |
| Isotype | Ig single chain of 5 VH (sc-5-VH) |
| Clonality | Monoclonal Antibody |
Title: Introducing Lunsekimig Biosimilar – Anti-IL13, Albumin mAb – Research Grade: A Novel Antibody Targeting IL-13 for Therapeutic Applications
Lunsekimig Biosimilar is a novel antibody, specifically designed to target interleukin-13 (IL-13) for therapeutic applications. IL-13 is a cytokine that plays a crucial role in the pathogenesis of various inflammatory diseases, making it an attractive therapeutic target. This biosimilar is a research-grade monoclonal antibody (mAb) that binds to IL-13 with high specificity and affinity. In this article, we will delve into the structure, activity, and potential applications of Lunsekimig Biosimilar.
Lunsekimig Biosimilar is a recombinant humanized mAb, meaning it is derived from human antibody sequences but has been modified to reduce immunogenicity. It consists of two heavy chains and two light chains, each with a variable region that specifically binds to IL-13. The constant region of the antibody is derived from human albumin, which provides stability and prolongs the half-life of the antibody in the body.
As an anti-IL-13 antibody, Lunsekimig Biosimilar binds to the IL-13 cytokine and prevents its interaction with its receptor, IL-13Rα1. This inhibits the downstream signaling pathways of IL-13, which are responsible for mediating inflammation and tissue damage. By blocking IL-13, Lunsekimig Biosimilar has the potential to reduce the severity of various inflammatory diseases.
Lunsekimig Biosimilar has shown promising results in preclinical studies for the treatment of various inflammatory diseases. IL-13 is known to play a role in the pathogenesis of asthma, atopic dermatitis, and inflammatory bowel disease. Therefore, Lunsekimig Biosimilar has been investigated as a potential treatment for these conditions. In a mouse model of asthma, Lunsekimig Biosimilar reduced airway inflammation and improved lung function. Similarly, in a mouse model of atopic dermatitis, it decreased skin inflammation and reduced the severity of symptoms. These preclinical studies demonstrate the potential of Lunsekimig Biosimilar as a therapeutic option for these diseases.
In addition to its potential in treating inflammatory diseases, Lunsekimig Biosimilar has also been studied for its anti-tumor activity. IL-13 has been shown to promote tumor growth and metastasis in certain cancers, making it an attractive target for cancer therapy. In preclinical studies, Lunsekimig Biosimilar has shown promising results in inhibiting tumor growth and metastasis in lung cancer and glioblastoma models. These findings suggest that Lunsekimig Biosimilar may have potential as a cancer therapeutic agent.
In conclusion, Lunsekimig Biosimilar is a novel antibody targeting IL-13 for therapeutic applications. Its structure, consisting of humanized antibody sequences and an albumin-derived constant region, provides specificity and stability. By blocking IL-13, Lunsekimig Biosimilar has the potential to reduce inflammation and tissue damage in various inflammatory diseases. It also shows promise as a potential treatment for certain cancers. Further clinical studies are needed to fully evaluate the efficacy and safety of Lunsekimig Biosimilar, but it holds great potential as a therapeutic option for IL-13-mediated diseases.
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