Prostatic Acid Phosphatase, Recombinant, Human, 6-His-tag (5'-nucleotidase, 5'-NT, Ecto-5'-nucleotidase, Thiamine Monophosphatase, TMPase, ACPP)

Prostatic Acid Phosphatase (ACPP) catalyzes the hydrolysis of a variety of phosphate monoesters, including phosphorylated proteins. The activity optimum of ACPP is in the pH range of 4-6, and the activity is inhibited by L(+)-tartrate. ACPP expression levels are highest in the prostate, with much lower expression in most other tissues. ACPP is a type I integral membrane protein of the plasma membrane and lysosomes, and a secreted form also exists. The concentration of ACPP is elevated in the circulation of prostate cancer patients, making the enzyme a marker for the progression of prostate cancer. Cellular ACPP has been shown to be a protein tyrosine phosphatase. Protein substrates include the epidermal growth factor receptor and HER-2. Cellular ACPP is considered to function as a tumor suppressor.\n\nSource:\nRecombinant corresponding to aa1-379 from human ACPP, fused to 6-His-tag at C-terminal expressed in mouse myeloma cell line, NS0.\n\nMolecular Weight:\n~41kD\n\nBiological Activity:\nMeasured by its ability to cleave a substrate, p-Nitrophenyl phosphate (pNPP).\n\nSpecific Activity:\n>100,000pmol/min/ug\n\nEndotoxin: ~1EU/1ug (LAL)\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

P9054-75C

Size

10ug

Form

Supplied as a liquid in Tris, sodium chloride.

Purity

~95% (SDS-PAGE)

References

1. Apostol, I. et al. (1985) Acta. Biochim. Pol. 32:187. 2. Schroeder, B. et al. (2007) Traffic 8:1676. 3. Gutman, E.B. et al. (1936) Am. J. Cancer 28:485. 4. Lin, M.F. and G.M. Clinton (1986) Biochem. J. 235:351. 5. Veeramani, S. et al. (2005) Endocr. Relat. Cancer 12:805