ACPP Human

Prostatic Acid Phosphatase is a dimeric glycoprotein with a molecular weight of approximately 100 kDa . The enzyme consists of two subunits and is known for its ability to cleave phosphate groups from various substrates. The catalytic activity of PAP is facilitated by specific residues, such as histidine (His) and aspartic acid (Asp), located in the cleft between its two domains .

PAP is clinically significant due to its role as a biomarker for prostate carcinoma. Elevated levels of PAP in the serum are often associated with prostate cancer, particularly in cases with bone metastasis . The enzyme’s activity is measured to monitor the progression of prostate cancer and to evaluate the effectiveness of therapeutic interventions .

Recombinant Human Prostatic Acid Phosphatase (rhPAP) is produced using recombinant DNA technology. The DNA sequence encoding human PAP is cloned and expressed in host cells, such as HEK293 cells, to produce the recombinant protein . The recombinant protein is then purified and characterized for various applications, including research and diagnostic purposes.

Recombinant PAP is used in various research studies to understand its role in prostate cancer and other physiological processes. It is also utilized in diagnostic assays to measure PAP levels in clinical samples. The recombinant form of PAP provides a consistent and reliable source of the enzyme for these applications .

Recombinant PAP is typically provided as a lyophilized powder and should be stored under sterile conditions at -20°C to -80°C. The protein is stable for up to twelve months when stored properly. It is recommended to avoid repeated freeze-thaw cycles to maintain its activity .