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pMD18-T Simple Vector is a high-efficiency TA cloning vector constructed from pUC18, of which the initial multiple cloning sites (MCS) were destroyed. Thus the cDNA should be amplified by PCR with primers containing a restriction site for subclone. Competent cells appropriate for pUC18 are also appropriated for the Vector, e.g. JM109, DH5α, TOP10. The pMD18-T Simple Vector is 2.6kb in size. Selection of the plasmid in E. coli is conferred by the ampicillin resistance gene. The coding sequence was inserted by TA cloning at site 425.
The coding sequence can be amplified by PCR with M13-47 and RV-M primers.
|Human ACPP ORF mammalian expression plasmid, C-GFPSpark tag||HG10959-ACG|
|Human ACPP ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10959-ACR|
|Human ACPP ORF mammalian expression plasmid, C-Flag tag||HG10959-CF|
|Human ACPP ORF mammalian expression plasmid, C-His tag||HG10959-CH|
|Human ACPP ORF mammalian expression plasmid, C-Myc tag||HG10959-CM|
|Human ACPP ORF mammalian expression plasmid, C-HA tag||HG10959-CY|
|Human ACPP ORF mammalian expression plasmid, Flag tag||HG10959-M-F|
|Human ACPP ORF mammalian expression plasmid, N-Flag tag||HG10959-NF|
|Human ACPP ORF mammalian expression plasmid, N-His tag||HG10959-NH|
|Human ACPP ORF mammalian expression plasmid, N-Myc tag||HG10959-NM|
|Human ACPP ORF mammalian expression plasmid, N-HA tag||HG10959-NY|
|Human ACPP natural ORF mammalian expression plasmid||HG10959-UT|
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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.