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Trontinemab Biosimilar – Anti-APP Abeta 1-40, 42;TFRC mAb – Research Grade

Reference:
Size

100µg, 1MG

Isotype

IgG1 Kappa;IgG1 Kappa

Brand

ProteoGenix

Product type

Primary Antibodies

Clonality

Monoclonal Antibody

Expression system

XtenCHO

Applications

Elisa, WB

Product nameTrontinemab Biosimilar - Anti-APP Abeta 1-40, 42;TFRC mAb - Research Grade
SpeciesBispecific Mixed Format with Domain Crossover
Expression systemXtenCHO
BufferPBS buffer PH7.5
Delivery conditionBlue ice (+4°C)
Delivery Time3-5 days if in stock; 3 week if production needed
Storage conditionstore at -80°C
BrandProteoGenix
Aliases /SynonymsTrontinemab,,APP Abeta 1-40, 42;TFRC,anti-APP Abeta 1-40, 42;TFRC
ReferencePX-TA1887
NoteFor research use only. Not suitable for clinical or therapeutic use.
IsotypeIgG1 Kappa;IgG1 Kappa
ClonalityMonoclonal Antibody

Description of Trontinemab Biosimilar - Anti-APP Abeta 1-40, 42;TFRC mAb - Research Grade

Introduction:

Trontinemab Biosimilar – Anti-APP Abeta 1-40, 42, TFRC mAb is a novel biosimilar antibody that targets amyloid-beta (Abeta) and transferrin receptor (TFRC) for the treatment of Alzheimer’s disease (AD). This biosimilar is a promising therapeutic agent with potential applications in both research and clinical settings. In this article, we will discuss the structure, activity, and potential applications of Trontinemab Biosimilar in detail.

Structure:

Trontinemab Biosimilar is a monoclonal antibody (mAb) that is produced by recombinant DNA technology. It is a biosimilar of the anti-Abeta antibody, Trontinemab, and has a similar structure and function. The antibody consists of two heavy chains and two light chains, which are connected by disulfide bonds. The heavy chains contain four constant domains (CH1-CH4) and one variable domain (VH), while the light chains contain two constant domains (CL) and one variable domain (VL). The variable domains are responsible for binding to specific targets, while the constant domains provide stability and effector functions.

Activity:

Trontinemab Biosimilar specifically targets two important proteins involved in the pathogenesis of AD – Abeta and TFRC. Abeta is a peptide that is known to form plaques in the brain, leading to neurodegeneration and cognitive decline in AD patients. Trontinemab Biosimilar binds to Abeta and prevents its aggregation, thereby reducing the formation of plaques and slowing down the progression of the disease. Additionally, TFRC is a receptor that is involved in the transport of iron into the brain. Iron accumulation has been linked to the development of AD, and by binding to TFRC, Trontinemab Biosimilar can regulate iron levels and potentially reduce the risk of AD.

Application:

Trontinemab Biosimilar has multiple potential applications in both research and clinical settings. In research, this biosimilar can be used to study the mechanisms of AD and to develop new therapeutic strategies. Its ability to target both Abeta and TFRC makes it a valuable tool for understanding the complex pathogenesis of AD. Trontinemab Biosimilar can also be used in preclinical studies to evaluate its efficacy and safety in animal models of AD.

In clinical settings, Trontinemab Biosimilar has the potential to be a game-changer in the treatment of AD. Currently, there is no cure for AD, and the available treatments only provide temporary relief of symptoms. Trontinemab Biosimilar, with its unique ability to target both Abeta and TFRC, has the potential to slow down the progression of the disease and improve the quality of life for AD patients. It can also be used in combination with other therapies to enhance their efficacy.

Conclusion:

In conclusion, Trontinemab Biosimilar – Anti-APP Abeta 1-40, 42, TFRC mAb – Research Grade is a promising therapeutic agent for the treatment of AD. Its unique structure and ability to target both Abeta and TFRC make it a valuable tool for research and a potential game-changer in clinical settings. Further studies and clinical trials are needed to fully understand the potential of this biosimilar in the treatment of AD.

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