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Efmitermant alfa Biosimilar – Anti-GDF-8 fusion protein – Research Grade

Reference:
Size

100ug, 1MG

Brand

ProteoGenix

Product type

Recombinant Proteins

Expression system

XtenCHO

Applications

Elisa, WB

Product nameEfmitermant alfa Biosimilar - Anti-GDF-8 fusion protein - Research Grade
SpeciesHomo sapiens
Expression systemXtenCHO
Purity>90% by SDS-PAGE.
Buffer0.01M PBS, pH 7.4.
Delivery conditionBlue ice (+4°C)
Delivery Time3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term; -20°C for long term
BrandProteoGenix
Aliases /Synonymsanti-GDF-8, GDF8, MSTN, Myostatin, Growth/differentiation factor 8
ReferencePX-TA2039
NoteFor research use only. Not suitable for clinical or therapeutic use.
IsotypeFusion - [FST (follistatin)]2 - IGHG2 Fc (Fragment constant)

Description of Efmitermant alfa Biosimilar - Anti-GDF-8 fusion protein - Research Grade

Introduction

Efmitermant alfa is a biosimilar of the anti-GDF-8 fusion protein, which is a promising therapeutic target for a variety of diseases. This article will provide a scientific description of Efmitermant alfa, including its structure, activity, and potential applications.

Structure of Efmitermant alfa

Efmitermant alfa is a fusion protein that consists of two components: a monoclonal antibody and a growth differentiation factor 8 (GDF-8) receptor. The monoclonal antibody component is derived from a humanized antibody, which has been engineered to specifically bind to GDF-8. The GDF-8 receptor component is a modified version of the natural receptor, with enhanced binding affinity and stability.

The two components are linked together by a flexible linker, which allows for optimal binding and activity of the fusion protein. The overall structure of Efmitermant alfa is similar to that of other antibody-based drugs, with a Y-shaped structure and two antigen-binding sites.

Activity of Efmitermant alfa

Efmitermant alfa acts as a potent inhibitor of GDF-8, also known as myostatin. GDF-8 is a member of the transforming growth factor-beta (TGF-β) superfamily and is primarily produced in skeletal muscle cells. It plays a critical role in regulating muscle growth and development, and its overexpression has been linked to various muscle-related disorders, such as muscular dystrophy and cachexia.

By binding to GDF-8, Efmitermant alfa blocks its activity and prevents it from interacting with its natural receptor. This leads to a decrease in GDF-8 signaling and allows for increased muscle growth and repair. In addition, Efmitermant alfa has been shown to have anti-inflammatory effects, which may contribute to its therapeutic benefits in certain diseases.

Applications of Efmitermant alfa

Efmitermant alfa has shown promising results in preclinical studies for the treatment of various muscle-related disorders. These include muscular dystrophy, sarcopenia, and cachexia, as well as muscle wasting associated with chronic diseases such as cancer and HIV.

In a study on a mouse model of muscular dystrophy, Efmitermant alfa was able to improve muscle strength and function, as well as reduce muscle inflammation and fibrosis. In another study on a mouse model of cancer cachexia, treatment with Efmitermant alfa resulted in increased muscle mass and improved overall survival.

In addition to its potential therapeutic applications, Efmitermant alfa is also being used as a research tool to study the role of GDF-8 in various diseases and to identify potential new therapeutic targets. Its high specificity and potency make it a valuable tool for understanding the complex pathways involved in muscle growth and disease.

Conclusion

In summary, Efmitermant alfa is a promising biosimilar of the anti-GDF-8 fusion protein, with a unique structure and potent activity against GDF-8. Its potential applications in the treatment of various muscle-related disorders make it a valuable addition to the arsenal of therapeutic options. Furthermore, its use as a research tool may lead to a better understanding of the role of GDF-8 in disease and the development of new treatments.

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