Cafelkibart Biosimilar – Anti-CKR-L1 mAb – Research Grade

Reference:
Product nameCafelkibart Biosimilar - Anti-CKR-L1 mAb - Research Grade
SourceCAS: 2851855-89-3
Origin speciesHuman
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
Aliases /Synonymsanti-CKR-L1, CMKBR8, C-C CKR-8, GPR-CY6, CCR8, CMKBRL2, TER1, CCR-8, Chemokine receptor-like 1, CKRL1, CDw198, GPRCY6, C-C chemokine receptor type 8, CC-CKR-8, CC chemokine receptor CHEMR1
ReferencePX-TA2175-100
NoteFor research use only. Not suitable for human use.
IsotypeIgG1-kappa
ClonalityMonoclonal Antibody

Description of Cafelkibart Biosimilar - Anti-CKR-L1 mAb - Research Grade

Cafelkibart Biosimilar – Anti-CKR-L1 mAb – Research Grade

Introduction

Cafelkibart Biosimilar – Anti-CKR-L1 mAb is a therapeutic antibody that has been developed as a biosimilar to the original anti-CKR-L1 monoclonal antibody (mAb). This biosimilar has been designed to target the same therapeutic target as the original antibody, but with improved structure and activity. In this article, we will discuss the structure, activity, and potential applications of this biosimilar in the field of therapeutic antibody research.

Structure of Cafelkibart Biosimilar – Anti-CKR-L1 mAb

The Cafelkibart Biosimilar – Anti-CKR-L1 mAb is a monoclonal antibody that is produced in a similar way to the original anti-CKR-L1 mAb. It is a protein molecule with a specific structure that allows it to bind to its therapeutic target, the CKR-L1 protein. The biosimilar has been engineered to have a similar structure to the original antibody, but with some modifications to improve its activity and stability.

The biosimilar consists of two heavy chains and two light chains that are connected by disulfide bonds. These chains are made up of amino acids, which are the building blocks of proteins. The amino acid sequence of the biosimilar has been carefully designed to ensure that it can bind specifically to the CKR-L1 protein and exert its therapeutic effects.

Activity of Cafelkibart Biosimilar – Anti-CKR-L1 mAb

The main activity of Cafelkibart Biosimilar – Anti-CKR-L1 mAb is to bind to the CKR-L1 protein and block its function. The CKR-L1 protein is a cell surface receptor that plays a role in inflammatory processes and has been implicated in various diseases such as rheumatoid arthritis and multiple sclerosis. By binding to the CKR-L1 protein, the biosimilar prevents it from interacting with its natural ligands and thus inhibits its signaling pathways.

The improved structure of the biosimilar allows it to have a higher binding affinity for the CKR-L1 protein compared to the original antibody. This means that lower doses of the biosimilar can be used to achieve the same therapeutic effect, reducing the risk of side effects and making it more cost-effective.

Applications of Cafelkibart Biosimilar – Anti-CKR-L1 mAb

The potential applications of Cafelkibart Biosimilar – Anti-CKR-L1 mAb are vast, as the CKR-L1 protein has been implicated in various diseases. The biosimilar can be used in the treatment of inflammatory conditions such as rheumatoid arthritis, multiple sclerosis, and psoriasis. It can also be used in the treatment of certain types of cancer, as the CKR-L1 protein has been found to play a role in tumor growth and metastasis.

Furthermore, the biosimilar can also be used in research studies to better understand the role of the CKR-L1 protein in different diseases and to develop new therapeutic approaches targeting this protein.

Conclusion

In conclusion, Cafelkibart Biosimilar – Anti-CKR-L1 mAb is a promising therapeutic antibody that has been developed as a biosimilar to the original anti-CKR-L1 mAb. Its improved structure and activity make it a powerful tool for targeting the CKR-L1 protein and potentially treating various diseases. With further research and clinical trials, this biosimilar has the potential to become a valuable addition to the field of therapeutic antibody research.

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