Recombinant Human PAP Protein

Beta LifeScience SKU/CAT #: BLA-6650P

Recombinant Human PAP Protein

Beta LifeScience SKU/CAT #: BLA-6650P
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Product Overview

Host Species Human
Accession P15309
Synonym 5' NT 5' nucleotidase 5'-NT 5'-nucleotidase Acid phosphatase prostate ACP 3 ACP3 acpP Ecto 5' nucleotidase Ecto-5'-nucleotidase PAP PPAP_HUMAN Prostatic acid phosphatase Prostatic acid phosphotase Thiamine monophosphatase TMPase
Description Recombinant Human PAP Protein was expressed in Baculovirus infected insect cells. It is a Full length protein
Source Baculovirus infected insect cells
Molecular Weight 45 kDa
Purity >95% SDS-PAGE.purified by using conventional chromatography techniques.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Specific activity is > 100,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37°C.
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.

Target Details

Target Function A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.; Tyrosine phosphatase that acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling. In addition to its tyrosine phosphatase activity has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor.; (Microbial infection) Forms amyloid beta-sheet fibrils in semen. These fibrils, termed SEVI (semen-derived enhancer of viral infection) capture HIV virions, attach them to target cells and enhance infection. SEVI amyloid fibrils are degraded by polyphenol epigallocatechin-3-gallate (EGCG), a constituent of green tea. Target cell attachment and enhancement of HIV infection is inhibited by surfen. Also similarly boosts XMRV (xenotropic murine leukemia virus-related virus) infection.
Subcellular Location [Isoform 1]: Secreted.; [Isoform 2]: Cell membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol.
Protein Families Histidine acid phosphatase family
Database References
Tissue Specificity Highly expressed in the prostate, restricted to glandular and ductal epithelial cells. Also expressed in bladder, kidney, pancreas, lung, cervix, testis and ovary. Weak expression in a subset of pancreatic islet cells, squamous epithelia, the pilosebaceou

Gene Functions References

  1. Enhanced TDPase and TMPase activities may contribute to the reduction of TDP level in AD patients. The results imply that an imbalance of phosphorylation-dephosphorylation related to thiamine and glucose metabolism may be a potential target for AD prevention and therapy. PMID: 28060825
  2. Thirteen single nucleotide polymorphism (SNPs) in acid phosphatase prostate (ACPP) were suggested as candidate causal alleles that underlie ACPP regulation and expression. PMID: 27357282
  3. we have measured the intramolecular diffusion of the full length and 8-residue deletion peptides at two different pHs and found a correlation with fibrillization lag time. These results can be explained by a simple kinetic model of the early stages of aggregation in which oligomerization is controlled by the rate of peptide reconfiguration. PMID: 27393931
  4. Prostatic acid phosphatase delays prostate cancer cell growth in G1 phase of the cell cycle. PMID: 26419820
  5. Studies suggest that understanding of prostatic acid phosphatase function and regulation of expression will have a significant impact on understanding prostate cancer (PCa) progression and therapy. PMID: 23698773
  6. Certain factors identified within semen, termed semen-derived enhancers of virus infection (SEVI), fragments of prostatic acid phosphatase, have been shown to significantly enhance HIV-1 infectivity. PMID: 25740984
  7. ACPP increases significantly in epithelial cells of ovarian carcinoma, which indicates that it may be a candidate biomarker for diagnosis of epithelia-derived ovarian cancer in women. PMID: 24829029
  8. Data indicate that hypoxia regulates prostatic acid phosphatase (PAP) through hypoxia-inducible factor 2 alpha (HIF2alpha) and from stimulated A2B adenosine receptors. PMID: 24434023
  9. GCNT1 is over-expressed in prostate cancer and is associated with higher levels of core 2 O-sLe(x) in PSA, PAP and MUC1 proteins. PMID: 24854630
  10. Data indicate that prostate acid phosphatase-based peptide vaccine PAP-114-128 peptide appears to be a relevant for the treatment of prostate cancer. PMID: 24338683
  11. Soluble ecto-5'-nucleotidase (5'-NT), alkaline phosphatase, and adenosine deaminase (ADA1) activities in neonatal blood favor elevated extracellular adenosine. PMID: 23897810
  12. PAPf39 is a 39 residue peptide fragment from human prostatic acidic phosphatase. Recombinant PAPf39 showed amyloid fibril formation. PMID: 23314347
  13. in the in vivo environment, PAP(248-286) is likely to form fibrils efficiently, thus providing an explanation for the presence of semen-derived enhancer of viral infection in human semen. PMID: 22354963
  14. Peptide fragments derived from N-proximal and C-proximal of the PAP form fibrillar structures and increase virion attachment to cells. PMID: 22090109
  15. PAP is strongly expressed in prostate cancer bone metastases in 7/7 patients, while prostate-specific antigen (PSA) is only weakly expressed. PMID: 22082367
  16. Our studies confirmed that, while prostatic acid phosphatase expression is not restricted to prostate tissues, its expression in other human tissues is approximately 1-2 orders of magnitude less than that observed in the prostate. PMID: 21487525
  17. Most of the features of PAP including gene regulation, gene/protein structure, functions, its role in tumor progression and evolutionary features are discussed. Review. PMID: 20645695
  18. prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth PMID: 20498373
  19. Data show that prostatic acid phosphatase(PAP) as a sensitive tumor marker for prostate cancer. PMID: 20392611
  20. PSAP might be predictive of tumor stage in incidental prostate cancer and represent a valuable adjunct for clinical decisions in terms of individual therapeutic management. PMID: 19301031
  21. The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP. The determined sequence of a 354 bp nucleotide fragment showed 90% identity with the corresponding sequence of human PAP. PMID: 19759923
  22. Effect of tartaric acid on conformation and stability of human prostatic phosphatase: an infrared spectroscopic and calorimetric study. PMID: 11833784
  23. Identification and characterization of regulatory elements of the human prostatic acid phosphatase promoter. PMID: 12032838
  24. analysis of mRNA levels in hyperplastic prostate stimulated with steroid hormones and growth factors PMID: 12362977
  25. equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate PMID: 12719131
  26. In dilute solutions, several active prostatic acid phosphatase species exist, which are involved in concentration-dependent dissociation/association equilibria PMID: 12962324
  27. Human prostatic acid phosphatase's regulatory regions were analyzed in transgenic mice and cell line transfections, in order to clarify the mechanisms of tissue-specific gene expression PMID: 14623260
  28. protein binding with Con A in seminal plasma PMID: 14690244
  29. Transcriptional activation of the prostatic acid phosphatase gene by NF-kappaB in human prostate cancer cells. PMID: 15240830
  30. Prostatic acid phosphatase inactivates lysophosphatidic acid in seminal plasma. PMID: 15280042
  31. analysis of prostatic acid phosphatase binding PMID: 15578709
  32. the GAAAATATGATA-like elements are involved in the transcriptional regulation of hPAP promoter constructs in prostatic cells. PMID: 15985366
  33. JFC1 differentially regulates the secretion of PSAP and PSA, and Rab27a and PI3K play a central role in the exocytosis of prostate-specific markers. PMID: 16004602
  34. 1,25D-mediated decreases in prostate cancer cells and C81 LN cell growth are in part due to decreases in tyrosine kinase signaling that result from up-regulation of cellular prostatic acid phosphatase. PMID: 16076555
  35. PAP (133-152) and PAP (173-192) were immunogenic and processed from whole PAP in HLA-DRB1*1501 tg mice. These peptides were capable of stimulating CD4 T lymphocytes from HLA-DRB1*1501-positive patients with granulomatous prostatitis and normal donors. PMID: 17455230
  36. Prostatic acid phosphatase is not a prostate specific target PMID: 17638863
  37. Suppresses pain by functioning as an ecto-5'-nucleotidase, activating A1-adenosine receptors in the dorsal spinal cord. PMID: 18940592
  38. presence of Prostatic Acid Phosphatase in breast cyst fluid may suggest its possible role in the development of breast cancer from cystic breast diseases PMID: 19108401
  39. Prostatic acid phosphatase boosts the infectivity of xenotropic murine leukemia virus-related virus. PMID: 19403677
  40. Report safety and immunological efficacy of a DNA vaccine encoding prostatic acid phosphatase in patients with stage D0 prostate cancer. PMID: 19636017
  41. molecular details of PAPf39 peptide fibril formation may aid in elucidating the mechanism of how PAPf39 fibrils are involved in HIV etiology PMID: 19902966


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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