E. coli-derived Human Prostatic Acid Phosphatase / ACPP fragment
Preparation
Produced in rabbits immunized with E. coli-derived Human Prostatic Acid Phosphatase / ACPP fragment, and purified by antigen affinity chromatography.
Source
Polyclonal Rabbit IgG
Purification
Protein A & Antigen Affinity
Formulation
PBS, pH7.0 with 0.03% Proclin300
Conjugate
Unconjugated
Form
Liquid
Shipping
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Storage
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Avoid repeated freeze-thaw cycles.
Anti-Prostatic Acid Phosphatase rabbit polyclonal antibody at 1:500 dilution Lane A: K562 Whole Cell Lysate Lane B: HeLa Whole Cell Lysate Lane C: HCT116 Whole Cell Lysate Lane D: Jurkat Whole Cell Lysate Lysates/proteins at 30 μg per lane. Secondary Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution. Developed using the ECL technique. Performed under reducing conditions. Predicted band size:45 kDa Observed band size:45 kDa (We are unsure as to the identity of these extra bands.)
Image 1 Alt Text
Human Prostatic Acid Phosphatase Western blot (WB) 30947
Anti-Prostatic Acid Phosphatase rabbit polyclonal antibody at 1:500 dilution Lane A: K562 Whole Cell Lysate Lane B: HeLa Whole Cell Lysate Lane C: HCT116 Whole Cell Lysate Lane D: Jurkat Whole Cell Lysate Lysates/proteins at 30 μg per lane. Secondary Goat Anti-Rabbit IgG (H+L)/HRP at 1/10000 dilution. Developed using the ECL technique. Performed under reducing conditions. Predicted band size:45 kDa Observed band size:45 kDa (We are unsure as to the identity of these extra bands.)
Image 2 Alt Text
Human Prostatic Acid Phosphatase Immunohistochemistry(IHC) 30948
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 is synthesized 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.
Research Areas
Phosphatases and Regulators
References
Hassan MI, et al. (2010) Structural and functional analysis of human prostatic acid phosphatase. Expert Rev Anticancer Ther. 10(7): 1055-68.
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.
Larsen RS, et al. (2009) A high throughput assay to identify small molecule modulators of prostatic acid phosphatase. Curr Chem Genomics. 3: 42-9.
Zimmermann H. (2009) Prostatic acid phosphatase, a neglected ectonucleotidase. Purinergic Signal. 5(3): 273-5.
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.
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.
Ostrowski WS, et al. (1994) Human prostatic acid phosphatase: selected properties and practical applications. Clin Chim Acta. 226(2): 121-9.