Prostatic Acid Phosphatase / ACPP Protein & Antibody

Acid Phosphatase, Prostate

Prostatic Acid Phosphatase / ACPP Products

Prostatic Acid Phosphatase / ACPP Protein, Recombinant

Molecule	Species	Description	Cat. No
Prostatic Acid Phosphatase/ACPP	Human	Prostatic Acid Phosphatase/ACPP Protein, Recombinant	10959-H08H
Prostatic Acid Phosphatase/ACPP	Mouse	ACPP / PSAP Protein, Recombinant	51018-M08H

Prostatic Acid Phosphatase / ACPP Antibody

Molecule	Species	Description	Cat. No
Prostatic Acid Phosphatase/ACPP	Human	Prostatic Acid Phosphatase/ACPP Antibody (Antigen Affinity Purified)	10959-RP02

Prostatic Acid Phosphatase / ACPP cDNA Clone

Molecule	Species	Description	Cat. No
Prostatic Acid Phosphatase/ACPP	Human	Prostatic Acid Phosphatase/ACPP cDNA Clone / ORF Clone	HG10959-M
Prostatic Acid Phosphatase/ACPP	Mouse	ACPP cDNA Clone / ORF Clone	MG51018-G

Prostatic Acid Phosphatase / ACPP Related Areas

Cancer>>Cancer Biomarkers>>Prostatic Acid Phosphatase/ACPP

Enzyme>>Phosphatase & Regulator>>Prostatic Acid Phosphatase/ACPP

Signal Transduction>>Phosphatase & Regulator>>Prostatic Acid Phosphatase/ACPP

Prostatic Acid Phosphatase / ACPP Alternative Names

Prostatic Acid Phosphatase, ACPP, ACP-3, ACP3, PAP, Acid Phosphatase, Prostate [Homo sapiens]

Prostatic Acid Phosphatase, Acpp, 9.104100899-104272570.1, A030005E02Rik, Lap, PAP, Ppal, Acid Phosphatase, Prostate [Mus musculus]

Prostatic Acid Phosphatase / ACPP Background

Prostatic acid phosphatase (PAP, or ACPP), also known as prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. As a non-specific phosphomonoesterase, Prostatic acid phosphatase synthetized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Prostatic acid phosphatase is a clinically important protein for its relevance as a biomarker of prostate carcinoma. Furthermore, it has a potential role in fertilization. The major action of PAP is to dephosphorylate macromolecules with the help of catalytic residues (His(12) and Asp(258)) that are located in the cleft between two domains. Cellular prostatic acid phosphatase (cPAcP), an authentic tyrosine phosphatase, is proposed to function as a negative growth regulator of prostate cancer (PCa) cells in part through its dephosphorylation of ErbB-2. cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Injection of the secretory isoform of PAP has potent antinociceptive effects in mouse models of chronic pain. This enzyme exhibits ecto-5'-nucleotidase activity, is widely distributed, and implicated in the formation of chronic pain. Additionally, PAP could be a target molecule in specific immunotherapy for patients with nonprostate adenocarcinomas including colon and gastric cancers.

Prostatic Acid Phosphatase / ACPP Related Studies

1. Hassan MI, et al. (2010) Structural and functional analysis of human prostatic acid phosphatase. Expert Rev Anticancer Ther. 10(7): 1055-68.
2. Chuang TD, et al. (2010) Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth. J Biol Chem. 285(31): 23598-606.
3. Larsen RS, et al. (2009) A high throughput assay to identify small molecule modulators of prostatic acid phosphatase. Curr Chem Genomics. 3: 42-9.
4. Zimmermann H. (2009) Prostatic acid phosphatase, a neglected ectonucleotidase. Purinergic Signal. 5(3): 273-5.
5. Wang Y, et al. (2005) Prostatic acid phosphatase as a target molecule in specific immunotherapy for patients with nonprostate adenocarcinoma. J Immunother. 28(6): 535-41.
6. Veeramani S, et al. (2005) Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer. Endocr Relat Cancer. 12(4): 805-22.
7. Ostrowski WS, et al. (1994) Human prostatic acid phosphatase: selected properties and practical applications. Clin Chim Acta. 226(2): 121-9.