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| Size | 100ug, 1MG |
|---|---|
| Brand | ProteoGenix |
| Product type | Recombinant Proteins |
| Clonality | Monoclonal Antibody |
| Expression system | XtenCHO |
| Applications | Elisa |
| Product name | Tarumase Biosimilar - Anti-peptidase S1 domain containing protein mAb - Research Grade |
|---|---|
| Source | CAS: 1243416-10-5 |
| Expression system | XtenCHO |
| Purity | >95% by SDS-PAGE. |
| Buffer | 0.01M PBS, pH 7.4. |
| Delivery condition | Blue ice (+4°C) |
| Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
| Storage condition | 4°C for short term; -20°C for long term |
| Brand | ProteoGenix |
| Reference | PX-TA2160 |
| Note | For research use only. Not suitable for human use. |
| Isotype | Lucilia sericata (common green bottle fly) peptidase S1 domaincontaining protein |
Introduction to Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb is a monoclonal antibody that has been developed as a biosimilar to the original Tarumase therapeutic antibody. This biosimilar is designed to target the peptidase S1 domain containing protein, which is a key enzyme involved in various disease processes. In this article, we will explore the structure, activity, and potential applications of this biosimilar in the field of therapeutics.
Structure of Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb is a monoclonal antibody that is composed of two identical heavy chains and two identical light chains. The heavy chains are approximately 150 kDa in size and consist of four constant domains (CH1, CH2, CH3, and CH4) and one variable domain (VH). The light chains are approximately 25 kDa in size and consist of two constant domains (CL and CL2) and one variable domain (VL). The heavy and light chains are held together by disulfide bonds.
The variable domains of Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb are responsible for its specificity and binding to the peptidase S1 domain containing protein. The constant domains, on the other hand, play a role in effector functions such as complement activation and binding to Fc receptors.
Activity of Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb binds to the peptidase S1 domain containing protein with high affinity and specificity. This binding inhibits the activity of the enzyme, which is involved in various disease processes such as inflammation, cancer, and autoimmune disorders.
In addition, Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb can also activate the complement system, leading to the destruction of target cells. This effector function is important in the treatment of certain types of cancer.
Application of Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb has potential applications in the treatment of various diseases. Its ability to inhibit the activity of the peptidase S1 domain containing protein makes it a promising therapeutic option for inflammatory diseases such as rheumatoid arthritis, psoriasis, and inflammatory bowel disease.
In addition, Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb has shown promising results in preclinical studies for the treatment of certain types of cancer, including breast cancer and lung cancer. Its ability to activate the complement system also makes it a potential therapy for certain types of blood cancers.
In conclusion, Tarumase Biosimilar – Anti-peptidase S1 domain containing protein mAb is a monoclonal antibody that has been developed as a biosimilar to the original Tarumase therapeutic antibody. Its structure, activity, and potential applications make it a promising therapeutic option for various diseases, particularly those involving the peptidase S1 domain containing protein. Further research and clinical trials are needed to fully evaluate the efficacy and safety of this biosimilar as a therapeutic agent.
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