|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive, Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
Human influenza hemagglutinin (HA) is a surface glycoprotein required for the infectivity of the human virus. The HA tag is derived from the HA-molecule corresponding to amino acids 98-106 has been extensively used as a general epitope tag in expression vectors. Many recombinant proteins have been engineered to express the HA tag, which does not appear to interfere with the bioactivity or the biodistribution of the recombinant protein. This tag facilitates the detection, isolation, and purification of the proteins.
The actual HA tag is as follows: 5' TAC CCA TAC GAT GTT CCA GAT TAC GCT 3' or 5' TAT CCA TAT GAT GTT CCA GAT TAT GCT 3' The amino acid sequence is: YPYDVPDYA.
|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 Gene cDNA clone plasmid||HG10959-M|
|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|
|Learn more about expression Vectors|
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.