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Coramitug Biosimilar – Anti-Transthyretin mAb – Research Grade

Reference:
Size

100ug, 1MG

Brand

ProteoGenix

Isotype

IgG1, kappa

Product type

Primary Antibodies

Clonality

Monoclonal Antibody

Expression system

XtenCHO

Applications

Elisa

Product nameCoramitug Biosimilar - Anti-Transthyretin mAb - Research Grade
SourceCAS: 2626841-92-5
Origin speciesChimeric
Expression systemXtenCHO
Purity>95% by SDS-PAGE.
Buffer0.01M PBS, pH 7.4.
Delivery conditionBlue ice (+4°C)
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term; -20°C for long term
BrandProteoGenix
ReferencePX-TA2113
NoteFor research use only. Not suitable for human use.
IsotypeIgG1-kappa
ClonalityMonoclonal Antibody

Description of Coramitug Biosimilar - Anti-Transthyretin mAb - Research Grade

Introduction

Coramitug Biosimilar – Anti-Transthyretin mAb – Research Grade is a novel monoclonal antibody that has been developed as a biosimilar to treat transthyretin-related amyloidosis (ATTR). This biosimilar is a highly specific and potent therapeutic agent that has been designed to target transthyretin (TTR) protein, which is the main cause of ATTR. In this article, we will discuss the structure, activity, and potential applications of Coramitug Biosimilar in the field of ATTR treatment.

Structure of Coramitug Biosimilar

Coramitug Biosimilar is a monoclonal antibody that has been engineered using recombinant DNA technology. It is a humanized antibody, which means that it contains both human and non-human components. The antibody 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 regions (CH1, CH2, CH3, and CH4) and one variable region (VH), while the light chains have one constant region (CL) and one variable region (VL). The variable regions of the antibody are responsible for binding to the TTR protein and initiating its therapeutic activity.

Activity of Coramitug Biosimilar

Coramitug Biosimilar has a high affinity for TTR protein and binds to it with high specificity. Once bound to TTR, the antibody triggers a series of downstream signaling events that lead to the inhibition of TTR aggregation and deposition in tissues, a hallmark of ATTR. This activity of Coramitug Biosimilar has been demonstrated in preclinical studies, where it has shown to effectively reduce TTR aggregation and improve tissue function in animal models of ATTR.

Moreover, Coramitug Biosimilar has also been shown to have a long half-life, allowing for less frequent dosing and potentially improving patient compliance. This is due to its Fc region, which is responsible for its binding to the neonatal Fc receptor (FcRn) and protecting it from degradation. This extended half-life also contributes to the sustained therapeutic effect of Coramitug Biosimilar, making it a promising candidate for the treatment of ATTR.

Application of Coramitug Biosimilar

Coramitug Biosimilar has the potential to be a game-changer in the treatment of ATTR. Currently, there are limited treatment options available for this disease, and most of them only provide symptomatic relief. With its highly specific and potent activity, Coramitug Biosimilar has the potential to not only slow down the progression of ATTR but also potentially reverse its effects.

In addition to its potential as a therapeutic agent, Coramitug Biosimilar can also be used as a research tool for studying the pathogenesis of ATTR. Its ability to inhibit TTR aggregation can help researchers gain a better understanding of the disease and potentially identify new therapeutic targets.

Conclusion

In summary, Coramitug Biosimilar – Anti-Transthyretin mAb – Research Grade is a novel monoclonal antibody that has been developed as a biosimilar to treat ATTR. Its unique structure and highly specific activity make it a promising candidate for the treatment of this debilitating disease. With further research and clinical trials, Coramitug Biosimilar has the potential to improve the lives of patients suffering from ATTR and pave the way for new therapeutic strategies for this disease.

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