Recombinant Mouse CLEC6A Protein, N-His

Reference: YMN00601
Product nameRecombinant Mouse CLEC6A Protein, N-His
Origin speciesMouse
Expression systemEukaryotic expression
Molecular weight21.78 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
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)
Fragment TypeIle44-Leu209
Aliases /SynonymsDC-associated C-type lectin 2, DECTIN2, Dendritic cell-associated C-type lectin 2, CLECSF10, CLEC6A, C-type lectin domain family 6 member A, C-type lectin superfamily member 10, Dectin-2
ReferenceYMN00601
NoteFor research use only.

Description of Recombinant Mouse CLEC6A Protein, N-His

Introduction to Recombinant Mouse CLEC6A Protein

Recombinant Mouse CLEC6A Protein, also known as C-type lectin domain family 6 member A, is a protein that plays a crucial role in the immune system. It is a type II transmembrane protein that belongs to the C-type lectin superfamily. This protein is encoded by the Clec6a gene and is highly conserved among mammals, with 92% sequence identity between human and mouse.

Structure of Recombinant Mouse CLEC6A Protein

The recombinant mouse CLEC6A protein is composed of 222 amino acids and has a predicted molecular weight of 24.7 kDa. It contains a single C-type lectin domain, a transmembrane region, and a cytoplasmic tail. The C-type lectin domain is responsible for the binding of carbohydrates and plays a crucial role in the recognition of pathogens.

The crystal structure of recombinant mouse CLEC6A protein has been determined, revealing a unique calcium-dependent binding site within the C-type lectin domain. This binding site allows the protein to interact with various ligands, including carbohydrates, lipids, and proteins, making it a versatile receptor in the immune system.

Activity of Recombinant Mouse CLEC6A Protein

The primary function of recombinant mouse CLEC6A protein is to act as a pattern recognition receptor (PRR) in the immune system. PRRs are essential for detecting and responding to pathogens, and CLEC6A is specifically involved in the recognition of fungal pathogens.

Upon binding to its ligands, recombinant mouse CLEC6A protein activates signaling pathways that lead to the production of pro-inflammatory cytokines and chemokines, which recruit immune cells to the site of infection. It also plays a role in phagocytosis, the process by which immune cells engulf and destroy pathogens.

In addition to its role in the immune system, recombinant mouse CLEC6A protein has been shown to have anti-tumor activity. It can recognize and bind to tumor-associated carbohydrates, leading to the activation of immune responses against cancer cells.

Application of Recombinant Mouse CLEC6A Protein

Recombinant mouse CLEC6A protein has a wide range of applications in both research and clinical settings. Its ability to recognize and bind to various ligands makes it a valuable tool for studying immune responses to pathogens and tumors.

In research, recombinant mouse CLEC6A protein is commonly used to study fungal infections, as it is a key receptor for the recognition of fungal pathogens. It is also used to investigate the role of C-type lectin receptors in immune responses and to study the mechanisms of phagocytosis.

In clinical settings, recombinant mouse CLEC6A protein has potential as a therapeutic target for the treatment of fungal infections and cancer. Researchers are currently exploring the use of CLEC6A as a biomarker for the diagnosis and prognosis of various diseases.

Conclusion

In summary, recombinant mouse CLEC6A protein is a versatile protein that plays a crucial role in the immune system. Its unique structure and activity make it an important receptor for the recognition of pathogens and tumors. With its various applications in research and potential therapeutic use, this protein continues to be a topic of interest in the scientific community.

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