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| Size | 100ug, 1MG |
|---|---|
| Brand | ProteoGenix |
| Product type | Recombinant Proteins |
| Expression system | XtenCHO |
| Applications | Elisa, WB |
| Product name | Rinvecalinase Alfa Biosimilar - Kallikrein-1 - Research Grade |
|---|---|
| Source | CAS: 2419877-37-3 |
| Buffer | 0.01M PBS, pH 7.4 |
| Delivery condition | Blue ice (+4°C) |
| Delivery Time | 3-5 days if in stock; 3 week if production needed |
| Storage condition | store at -80°C |
| Brand | ProteoGenix |
| Aliases /Synonyms | anti-Kallikrein-1, Kidney/pancreas/salivary gland kallikrein, Tissue kallikrein, KLK1 |
| Reference | PX-TA1993 |
| Note | For research use only. Not suitable for clinical or therapeutic use. |
| Isotype | Human kallikrein-1/KLK1 mature form |
Rinvecalinase Alfa Biosimilar, also known as Kallikrein-1, is a research grade antibody that has shown promising results in the treatment of certain diseases. This biosimilar is a recombinant version of the naturally occurring protein, kallikrein-1, which plays a crucial role in various physiological processes such as blood pressure regulation, inflammation, and tissue repair. In this article, we will explore the structure, activity, and potential applications of Rinvecalinase Alfa Biosimilar.
Rinvecalinase Alfa Biosimilar is a monoclonal antibody that is produced by recombinant DNA technology. It is composed of two identical heavy chains and two identical light chains, each consisting of a variable and a constant region. The variable regions of the heavy and light chains are responsible for recognizing and binding to the target molecule, kallikrein-1. The constant regions of the antibody provide stability and effector functions.
The amino acid sequence of Rinvecalinase Alfa Biosimilar is highly similar to that of the naturally occurring kallikrein-1, ensuring its specificity and efficacy in targeting the same molecule. The recombinant production of this biosimilar allows for a consistent and reliable supply, making it a valuable tool for research and potential therapeutic use.
Rinvecalinase Alfa Biosimilar acts as a potent inhibitor of kallikrein-1 activity. Kallikrein-1 is an enzyme that cleaves kininogen, a precursor protein, to produce bradykinin, a potent vasodilator and inflammatory mediator. Inhibition of kallikrein-1 by Rinvecalinase Alfa Biosimilar leads to a decrease in bradykinin levels, resulting in reduced inflammation and blood pressure regulation.
In addition to its inhibitory activity, Rinvecalinase Alfa Biosimilar also has the ability to bind to kallikrein-1 and prevent its interaction with other molecules, further limiting its activity. This dual mechanism of action makes Rinvecalinase Alfa Biosimilar a promising candidate for the treatment of diseases where kallikrein-1 plays a significant role.
The potential therapeutic applications of Rinvecalinase Alfa Biosimilar are vast, as kallikrein-1 is involved in various diseases and conditions. One of the most promising areas of research is in the treatment of hereditary angioedema (HAE), a rare genetic disorder characterized by recurrent episodes of swelling in various parts of the body. HAE is caused by a deficiency or dysfunction of C1 inhibitor, a protein that regulates kallikrein-1 activity. By inhibiting kallikrein-1, Rinvecalinase Alfa Biosimilar can potentially prevent HAE attacks and improve the quality of life for patients.
Rinvecalinase Alfa Biosimilar may also have therapeutic potential in other conditions such as inflammatory diseases, cardiovascular diseases, and cancer. Inflammation is a hallmark of many diseases, and kallikrein-1 has been shown to play a role in the inflammatory response. By inhibiting kallikrein-1, Rinvecalinase Alfa Biosimilar may help reduce inflammation and alleviate symptoms in conditions such as rheumatoid arthritis and asthma.
Furthermore, kallikrein-1 has been implicated in cardiovascular diseases such as hypertension and heart failure. By inhibiting kallikrein-1, Rinvecalinase Alfa Biosimilar may help regulate blood pressure and improve heart function. Additionally, kallikrein-1 has been found to be overexpressed in certain types of cancer, making it a potential therapeutic target
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