Prostatic Acid Phosphatase (mouse, recombinant)

Prostatic acid phosphatase is a member of the protein tyrosine phosphatase (PTP) family.¹ It exists as a homodimer and each monomer is composed of a signal peptide, which, once cleaved, produces a catalytically active enzyme, and two domains where the larger domain contains an α/β-hydrolase fold and the smaller domain contains mostly α-helices. Alternative splicing of the gene encoding prostatic acid phosphatase, Acp3, generates a secreted form that is expressed in prostate tissues and semen, and a transmembrane form that is expressed in several tissues.^2,3,4 In addition to its phosphatase activity, prostatic acid phosphatase also has ectonucleotidase activity against AMP, ADP, and ATP in a pH-dependent manner.⁵ Intrathecal administration of recombinant mouse prostatic acid phosphatase has antinociceptive activity in a mouse model of inflammatory pain induced by complete Freund’s adjuvant (CFA). Serum levels of prostatic acid phosphatase are increased in patients with prostate cancer and vaginal prostatic acid phosphatase activity has been used as a marker of sexual abuse.^1,6 Cayman’s Prostatic Acid Phosphatase (mouse, recombinant) protein consists of 361 amino acids, has a calculated molecular weight of 42 kDa, and a predicted N-terminus of Lys32 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 47 kDa due to glycosylation.

WARNING This product is not for human or veterinary use.

1. Muniyan, S., Chaturvedi, N.K., Dwyer, J.G., et al. Human prostatic acid phosphatase: Structure, function and regulation. Int. J. Mol. Sci. 14(5), 10438-10464 (2013).

2. Vihko, P., Virkkunen, P., Henttu, P., et al. Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 236(2), 275-281 (1988).

3. Vaulbourdolle, M., Clavel, J.P., Cynober, L., et al. Acid phosphatase and zinc in semen of subjects with no clinical evidence of prostatic disease. Clin. Chem. 31(6), 878-880 (1985).

4. Quintero, I.B., Araujo, C.L., Pulkka, A.E., et al. Prostatic acid phosphatase is not a prostate specific target. Cancer Res. 67(14), 6549-6554 (2007).

5. Sowa, N.A., Vadakkan, K.I., and Zylka, M.J. Recombinant mouse PAP has pH-dependent ectonucleotidase activity and acts through A₁-adenosine receptors to mediate antinociception. PLoS One 4(1), e4248 (2009).

6. Peonim, V., Worasuwannarak, W., Sujirachato, K., et al. Comparison between prostate specific antigen and acid phosphatase for detection of semen in vaginal swabs from raped women. J. Forensic Leg. Med. 20(6), 578-581 (2013).