Prostatic acid Phosphatase/ACPP Protein, Human (HEK293, GFP-His)

Prostatic acid phosphatase (ACPP) functions as a multifunctional tyrosine phosphatase under acidic conditions (pH 4-6), dephosphorylating a variety of substrates, including orthophosphate monoesters. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma. Prostatic acid Phosphatase/ACPP Protein, Human (HEK293, GFP-His) is the recombinant human-derived Prostatic acid Phosphatase/ACPP protein, expressed by HEK293 , with C-His, GFP labeled tag.

Prostatic acid phosphatase (ACPP) is a non-specific tyrosine phosphatase that operates under acidic conditions (pH 4-6), demonstrating its versatility in dephosphorylating a diverse array of substrates, including alkyl, aryl, and acyl orthophosphate monoesters, as well as phosphorylated proteins. Notably, ACPP exhibits lipid phosphatase activity, contributing to the inactivation of lysophosphatidic acid in seminal plasma. Functioning as a tumor suppressor in prostate cancer, ACPP plays a crucial role in dephosphorylating ERBB2 and deactivating MAPK-mediated signaling, thereby exerting control over cellular processes implicated in cancer progression. Beyond its tyrosine phosphatase activity, ACPP showcases ecto-5'-nucleotidase activity in dorsal root ganglion neurons, generating adenosine from AMP. This additional function suggests a role in pain modulation, where adenosine acts as a pain suppressor, emphasizing the multifaceted nature of ACPP in cellular processes.

Human

HEK293

C-His;GFP

P15309-2 (K33-K382)

55  [NCBI]

Partial

KELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQVLK

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.