PIR Human

Pirin is composed of 290 amino acids and has a molecular weight of approximately 34.3 kDa . The recombinant form of human Pirin is often produced in E. coli and includes an N-terminal His-tag to facilitate purification . The protein is typically purified using conventional chromatography techniques and is available in a highly pure form (>95% purity by SDS-PAGE) .

Pirin is known to interact with several important proteins, including nuclear factor I/CCAAT box transcription factor and B cell lymphoma 3-encoded oncoprotein . These interactions suggest that Pirin may act as a transcriptional cofactor, playing a role in the regulation of DNA transcription and replication . Additionally, Pirin has been implicated in various cellular processes, including oxidative stress response and apoptosis.

Recombinant human Pirin is widely used in research to study its role in cellular processes and its interactions with other proteins. It is also used in structural biology studies to understand its β-barrel structure and how it binds to iron .

Recombinant human Pirin is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain the protein’s stability . The protein is usually formulated in a buffer containing Tris-HCl, glycerol, NaCl, and DTT to ensure its stability during storage .