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Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade

Reference:
Size

100ug, 1MG

Brand

ProteoGenix

Isotype

IgG2-G4-kappa

Product type

Primary Antibodies

Clonality

Monoclonal Antibody

Expression system

XtenCHO

Applications

Elisa

Product nameOmoprubart Biosimilar - Anti-CPAMD4 mAb - Research Grade
SourceCAS: 2763342-87-4
Origin speciesHomo sapiens
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-TA2130
NoteFor research use only. Not suitable for human use.
IsotypeIgG2/G4-kappa
ClonalityMonoclonal Antibody

Description of Omoprubart Biosimilar - Anti-CPAMD4 mAb - Research Grade

Introduction to Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade

Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade is a novel monoclonal antibody (mAb) that has been developed as a biosimilar to the existing anti-CPAMD4 mAb. This biosimilar has been specifically designed for research purposes and offers a cost-effective alternative to the original anti-CPAMD4 mAb. In this article, we will discuss the structure, activity and potential applications of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade.

Structure of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade

Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade is a recombinant humanized IgG1 monoclonal antibody. It is composed of two heavy chains and two light chains, each containing a variable region and a constant region. The variable regions of the heavy and light chains are responsible for binding to the target protein, CPAMD4.

The heavy chain variable region of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade is derived from a human antibody, while the light chain variable region is derived from a mouse antibody. This allows for a high affinity and specificity towards CPAMD4, while also reducing the risk of immune reactions in humans.

Activity of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade

Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade specifically targets and binds to CPAMD4, a protein that is overexpressed in certain types of cancer, including breast, lung and colorectal cancer. By binding to CPAMD4, this mAb inhibits its activity and disrupts the signaling pathways involved in cancer growth and progression.

In addition to its anti-

cancer activity, Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade has also shown potential in treating autoimmune diseases. CPAMD4 has been implicated in the development of autoimmune disorders, and by targeting and neutralizing this protein, this mAb can potentially alleviate symptoms and improve patient outcomes.

Title: Potential Applications of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade The primary application of Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade is in cancer research. Its ability to specifically target and inhibit CPAMD4 makes it a valuable tool for studying the role of this protein in cancer development and progression. It can also be used in pre-clinical studies to assess the efficacy of CPAMD4 as a therapeutic target for cancer treatment.

In addition to cancer research, Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade also has potential applications in autoimmune disease research. Its ability to neutralize CPAMD4 can aid in understanding the role of this protein in autoimmune disorders and could potentially lead to the development of new treatments for these diseases.

Conclusion

Omoprubart Biosimilar – Anti-CPAMD4 mAb – Research Grade is a novel monoclonal antibody that offers a cost-effective alternative to the original anti-CPAMD4 mAb. Its structure, activity and potential applications make it a valuable tool in cancer and autoimmune disease research. As more studies are conducted, this biosimilar has the potential to pave the way for new treatments and advancements in these fields.

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