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Brand: ProteoGenix

Libevitug Biosimilar – Anti-Large envelope protein mAb – Research Grade

  • PX-TA2196
Clonality:
Monoclonal Antibody
Isotype:
IgG1, lambda2

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Libevitug Biosimilar - Anti-Large envelope protein mAb - Research Grade

Libevitug Biosimilar - Anti-Large envelope protein mAb - Research Grade

Product name Libevitug Biosimilar - Anti-Large envelope protein mAb - Research Grade
Source CAS: 2817665-64-6
Origin species Hepatitis B virus genotype A2 subtype adw (isolate Japan/Nishioka/1983) (HBV-A)
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
Aliases /Synonyms anti-Large envelope protein, L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen; S
Reference PX-TA2196-100
Note For research use only. Not suitable for human use.
Isotype IgG1, lambda2
Clonality Monoclonal Antibody

Introduction

Libevitug Biosimilar is a therapeutic antibody that targets the large envelope protein (LGP) of a virus. This research grade antibody is a highly specific and potent tool for studying the structure, activity, and potential therapeutic applications of LGP in viral infections. In this article, we will discuss the structure, activity, and potential applications of Libevitug Biosimilar in detail.

Structure of Libevitug Biosimilar

Libevitug Biosimilar is a monoclonal antibody (mAb) that is produced by recombinant DNA technology. It is composed of two heavy chains and two light chains, each with a specific amino acid sequence. The heavy chains are connected to each other by disulfide bonds, while the light chains are connected to the heavy chains by both disulfide bonds and non-covalent interactions. The variable regions of the heavy and light chains form the antigen-binding site, which is responsible for the specificity of Libevitug Biosimilar towards LGP.

Activity of Libevitug Biosimilar

The primary function of Libevitug Biosimilar is to bind to LGP and inhibit its activity. LGP is a key protein involved in the entry and replication of certain viruses, making it an attractive therapeutic target. By binding to LGP, Libevitug Biosimilar prevents the virus from entering and infecting host cells, thus inhibiting viral replication and spread.

In addition to its inhibitory activity, Libevitug Biosimilar also has the ability to induce antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC). These mechanisms involve the activation of immune cells, such as natural killer cells and macrophages, to target and destroy virus-infected cells. This dual mechanism of action makes Libevitug Biosimilar a potent and effective therapeutic tool against LGP-targeting viruses.

Potential Applications of Libevitug Biosimilar

Libevitug Biosimilar has potential applications in both research and clinical settings. In research, it can be used to study the structure and function of LGP and its role in viral infections. The high specificity and potency of Libevitug Biosimilar make it a valuable tool for understanding the molecular mechanisms of LGP-mediated viral entry and replication.

In clinical settings, Libevitug Biosimilar has the potential to be developed as a therapeutic agent for treating viral infections. By targeting LGP, it can potentially inhibit the entry and replication of a wide range of viruses, including hepatitis B and C, HIV, and influenza. Furthermore, the ability of Libevitug Biosimilar to induce ADCC and CDC can also help in clearing virus-infected cells and reducing viral load in patients.

Conclusion

In summary, Libevitug Biosimilar is a highly specific and potent therapeutic antibody that targets the large envelope protein of viruses. Its structure, activity, and potential applications make it a valuable tool for studying LGP and its role in viral infections. Furthermore, the dual mechanism of action of Libevitug Biosimilar makes it a promising candidate for the development of therapeutic interventions against LGP-targeting viruses.

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