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CUSABIO Transmembrane Proteins: Driving Breakthroughs in Therapeutic Antibody Discovery


News provided by

CUSABIO

Oct 31, 2024, 08:32 ET

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HOUSTON, Oct. 31, 2024 /PRNewswire/ -- In recent years, antibody therapies have seen rapid advancements, becoming pivotal treatments for cancer, infectious diseases, and autoimmune disorders. Innovations such as monoclonal antibodies (mAbs), bispecific antibodies (bsAbs), and antibody-drug conjugates (ADCs) have significantly propelled the biopharmaceutical industry forward.

Transmembrane proteins play a critical role in the development of antibody therapies in several ways:

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The function of transmembrane proteins
The function of transmembrane proteins
Three multi-transmembrane protein technology platforms
Three multi-transmembrane protein technology platforms

Target Selection
Transmembrane proteins are frequently the primary targets of antibody therapies. Located on the cell membrane, these proteins are readily accessible for antibodies to bind to in the extracellular environment, triggering specific biological effects. For example, CD20 and CLDN18.2 are overexpressed in certain diseases and have become ideal targets for precision therapies.

Drug Design
Transmembrane proteins, especially those with multiple transmembrane domains, present significant challenges for antibody drug design due to their complex structures. A deep understanding of the 3D structure and functional mechanisms of these proteins is essential for developing novel antibody drugs. Notably, antibodies targeting G protein-coupled receptors (GPCRs) and ion channels, both of which are transmembrane proteins, are gaining increasing attention in drug development.

Therapeutic Mechanisms
Transmembrane proteins are integral to cell signaling and immune regulation. Antibodies can influence disease progression by binding to these proteins and either inhibiting or activating downstream signaling pathways. Additionally, antibodies can recruit the immune system, such as through antibody-dependent cellular cytotoxicity (ADCC), to target and destroy cells expressing specific transmembrane proteins.

Application of Bispecific Antibodies
Bispecific antibodies can bind to two different targets simultaneously, with one target often being a transmembrane protein. This approach enhances antibody specificity and improves therapeutic efficacy. In cancer therapy, for instance, bispecific antibodies can direct T cells to tumor cells by leveraging interactions between transmembrane proteins and T cell receptors, thereby boosting immune responses.

Nearly 30% of genes in the human genome encode transmembrane proteins, and approximately 50% of currently known drug targets are transmembrane proteins, making them the most prominent family of therapeutic targets.

However, the expression and purification of transmembrane proteins present significant challenges. These include limited extracellular epitopes, the need for isolation of pure proteins in their native conformation, and difficulties in expressing full-length, properly folded integral membrane proteins.

As a leading protein manufacturer, CUSABIO provides three advanced technology platforms—virus-like particles (VLPs), detergent micelles, and Nanodiscs—to support the development of transmembrane proteins.

Since establishing these platforms, CUSABIO has successfully produced over 470 proteins, including 130+ transmembrane proteins (TPs) with 1-15 transmembrane domains and toxic proteins that are difficult to express using traditional E. coli systems. Additionally, CUSABIO has successfully produced high molecular weight proteins (130-140 kDa) with multiple transmembrane domains. To date, CUSABIO has completed more than 100 projects, offering screening services targeting multi-pass transmembrane proteins.

CUSABIO remains committed to delivering high-quality, risk-free transmembrane proteins to researchers, continuing to facilitate advancements in biomedical research. Explore CUSABIO transmembrane protein solutions today.

Contact:
Rosie Liu
3013634651
[email protected]

SOURCE CUSABIO

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