CNPY3 Human

CNPY3 is a 271 amino acid protein with a molecular mass of approximately 29.9 kDa. It is produced as a single, non-glycosylated polypeptide chain in Escherichia coli (E. coli) and is often fused to a 23 amino acid His-tag at the N-terminus for purification purposes . The protein solution typically contains 20 mM Tris-HCl buffer (pH 8.0), 0.15 M NaCl, 10% glycerol, and 1 mM DTT .

CNPY3 functions as a co-chaperone for HSP90B1, a heat shock protein. It is specifically required for the proper folding of Toll-like receptors, excluding TLR3, and controls their exit from the endoplasmic reticulum . This process is vital for the immune system’s ability to recognize and respond to pathogens.

The role of CNPY3 in the immune system is significant due to its involvement in the folding and export of TLRs. TLRs are a class of proteins that play a key role in the innate immune system by recognizing pathogen-associated molecular patterns (PAMPs) and initiating immune responses . Without proper folding and functioning of TLRs, the immune system’s ability to detect and respond to infections would be compromised.

Mutations or dysregulation of the CNPY3 gene have been associated with various immune-related disorders. For instance, CNPY3 is linked to Developmental and Epileptic Encephalopathy 60 and West Syndrome . These associations highlight the importance of CNPY3 in maintaining immune system homeostasis and its potential as a therapeutic target.

Recombinant CNPY3 is widely used in research to study its role in TLR folding and immune responses. It is also utilized in various assays and experiments to understand its interactions with other proteins and its impact on immune signaling pathways .