Recombinant Human CLEC3B, N-His

Reference: YHC16901
Product nameRecombinant Human CLEC3B, N-His
Uniprot IDP05452
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsTetranectin, Plasminogen kringle 4-binding protein, CLEC3B, TN, C-type lectin domain family 3 member B, TNA
ReferenceYHC16901
NoteFor research use only

Description of Recombinant Human CLEC3B, N-His

Introduction

Recombinant Human CLEC3B, N-His is a protein that has gained significant attention in the field of drug discovery due to its potential as a drug target. This protein belongs to the C-type lectin domain family and is involved in various biological processes, making it a promising candidate for therapeutic interventions. In this article, we will discuss the structure, activity, and potential applications of Recombinant Human CLEC3B, N-His.

Structure of Recombinant Human CLEC3B, N-His

Recombinant Human CLEC3B, N-His is a 33 kDa glycoprotein that consists of 312 amino acids. It is composed of a single C-type lectin domain, which is responsible for its binding activity. This domain is characterized by a conserved calcium-binding site and a carbohydrate recognition site, which enables the protein to interact with various ligands. The N-terminal of the protein contains a polyhistidine tag (N-His), which allows for easy purification and detection of the protein.

Activity of this protein

Recombinant Human CLEC3B, N-His has been found to have multiple activities in different biological processes. One of its main functions is its ability to bind to various glycosaminoglycans (GAGs) such as heparin and chondroitin sulfate. This binding activity is essential for the regulation of cell adhesion, migration, and proliferation. Additionally, Recombinant Human CLEC3B, N-His has been shown to interact with other proteins, including fibronectin and collagen, which are involved in extracellular matrix organization and tissue repair.

Furthermore, studies have demonstrated that Recombinant Human CLEC3B, N-His has anti-inflammatory properties. It has been shown to inhibit the production of pro-inflammatory cytokines and chemokines, suggesting its potential as a therapeutic agent for inflammatory diseases.

Potential Applications of Recombinant Human CLEC3B, N-His

Recombinant Human CLEC3B, N-His has shown great potential for various applications in the field of drug discovery. Its ability to bind to GAGs and other proteins makes it a promising drug target for diseases involving abnormal cell adhesion and migration. This includes cancer, as the dysregulation of cell adhesion and migration is a hallmark of cancer progression.

Moreover, the anti-inflammatory properties of Recombinant Human CLEC3B, N-His make it a potential candidate for the treatment of inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. Its ability to inhibit the production of pro-inflammatory cytokines and chemokines can help reduce inflammation and alleviate symptoms in these conditions.

In addition to its potential as a therapeutic target, Recombinant Human CLEC3B, N-His also has applications in research and diagnostics. Its binding activity to GAGs and other proteins can be utilized in various assays and experiments to study cell adhesion and migration. The N-His tag also allows for easy purification and detection of the protein, making it a valuable tool in protein purification and detection techniques.

Conclusion

In conclusion, Recombinant Human CLEC3B, N-His is a promising protein with multiple activities and potential applications. Its structure, activity, and potential as a drug target make it an attractive candidate for therapeutic interventions in various diseases. Further research on this protein may uncover its full potential and lead to the development of novel treatments for a range of diseases.

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