acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
Greater than 95.0% as determined by SDS-PAGE.
ACPP Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (32-381 aa) and having a molecular mass of 41.3kDa.
ACPP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Prostatic Acid Phosphatase (ACPP) belongs to the histidine acid phosphatase protein family. It catalyzes the hydrolysis of phosphate monoesters and phosphorylated proteins. ACPP exhibits optimal activity within a pH range of 4-6. Its catalytic activity is inhibited by L(+)-tartrate. Notably, ACPP can function as a lipid phosphatase, demonstrating the ability to inhibit lysophosphatidic acid in seminal plasma.
ACPP Mouse, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 356 amino acids (32-381 aa) and has a molecular weight of 41.3kDa. The protein includes a 6 amino acid His tag fused at the C-terminus and is purified using proprietary chromatographic techniques.
The ACPP solution is provided at a concentration of 0.5mg/ml in a buffer consisting of 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
The specific activity of the enzyme is measured to be greater than 80,000 units per milligram (unit/mg). Specific activity is defined as the amount of enzyme required to hydrolyze 1.0 nanomole of p-nitrophenyl phosphate (pNPP) per minute at a pH of 5.0 and a temperature of 37°C.
acid phosphatase, prostate, ACP3, ACP-3, ACPP, EC 3.1.3.2, PAP, Prostatic Acid Phosphatase, prostatic acid phosphatase, 5-nucleotidase, 5'-NT, Acid phosphatase 3, Ecto-5'-nucleotidase, Fluoride-resistant acid phosphatase, FRAP, Thiamine monophosphatase, TMPase, A030005E02Rik, Lap, PAP, Ppal.
KELKFVTLVF RHGDRGPIET FPTDPITESS WPQGFGQLTQ WGMEQHYELG SYIRKRYGRF LNDTYKHDQI YIRSTDVDRT LMSAMTNLAA LFPPEGISIW NPRLLWQPIP VHTVSLSEDR LLYLPFRDCP RFEELKSETL ESEEFLKRLH PYKSFLDTLS SLSGFDDQDL FGIWSKVYDP LFCESVHNFT LPSWATEDAM IKLKELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILKNMK LATQPQKYKK LVMYSAHDTT VSGLQMALDV YNGVLPPYAS CHMMELYHDK GGHFVEMYYR NETQNEPYPL TLPGCTHSCP LEKFAELLDP VISQDWATEC MATSSHQGRN HHHHHH.
The recombinant mouse prostatic acid phosphatase is typically expressed in HEK293 cells. The DNA sequence encoding the mouse ACPP isoform 1 (Met1-Arg381) is expressed with a C-terminal polyhistidine tag . The recombinant protein consists of 361 amino acids and has a predicted molecular mass of 42 kDa. However, due to glycosylation, its apparent molecular mass is approximately 47 kDa when analyzed by SDS-PAGE under reducing conditions .
Prostatic acid phosphatase is a non-specific phosphomonoesterase that is synthesized and secreted into seminal plasma under androgenic control . The enzyme is a dimer with a molecular weight of around 100 kDa. Its primary function is to dephosphorylate macromolecules, which is facilitated by catalytic residues (His12 and Asp258) located in the cleft between two domains .
Cellular prostatic acid phosphatase (cPAcP) functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells. It dephosphorylates HER-2/ErbB-2/Neu (human epidermal growth factor receptor-2) at the phosphotyrosine residues . This activity is proposed to function as a negative growth regulator of prostate cancer cells, in part through its dephosphorylation of ErbB-2 .