Recombinant Human Prostatic Acid Phosphatase (ACP3) Protein (GFP-His)

Name: Recombinant Human Prostatic Acid Phosphatase (ACP3) Protein (GFP-His)
Brand: Beta LifeScience
SKU: BLC-00254P
Price: 240.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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100ug

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Product Overview

Description	Recombinant Human Prostatic Acid Phosphatase (ACP3) Protein (GFP-His) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P15309
Target Symbol	ACP3
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-GFP-10His
Target Protein Sequence	KELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQVLK
Expression Range	33-382aa
Protein Length	Partial of Isoform 2
Mol. Weight	70.6 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 125 OMIM: 171790 KEGG: hsa:55 STRING: 9606.ENSP00000323036 UniGene: PMID: 28060825 Thirteen single nucleotide polymorphism (SNPs) in acid phosphatase prostate (ACPP) were suggested as candidate causal alleles that underlie ACPP regulation and expression. PMID: 27357282 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 Prostatic acid phosphatase delays prostate cancer cell growth in G1 phase of the cell cycle. PMID: 26419820 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 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 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 Data indicate that hypoxia regulates prostatic acid phosphatase (PAP) through hypoxia-inducible factor 2 alpha (HIF2alpha) and from stimulated A2B adenosine receptors. PMID: 24434023 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 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 Soluble ecto-5'-nucleotidase (5'-NT), alkaline phosphatase, and adenosine deaminase (ADA1) activities in neonatal blood favor elevated extracellular adenosine. PMID: 23897810 PAPf39 is a 39 residue peptide fragment from human prostatic acidic phosphatase. Recombinant PAPf39 showed amyloid fibril formation. PMID: 23314347 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 Peptide fragments derived from N-proximal and C-proximal of the PAP form fibrillar structures and increase virion attachment to cells. PMID: 22090109 PAP is strongly expressed in prostate cancer bone metastases in 7/7 patients, while prostate-specific antigen (PSA) is only weakly expressed. PMID: 22082367 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 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 prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth PMID: 20498373 Data show that prostatic acid phosphatase(PAP) as a sensitive tumor marker for prostate cancer. PMID: 20392611 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 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 Effect of tartaric acid on conformation and stability of human prostatic phosphatase: an infrared spectroscopic and calorimetric study. PMID: 11833784 Identification and characterization of regulatory elements of the human prostatic acid phosphatase promoter. PMID: 12032838 analysis of mRNA levels in hyperplastic prostate stimulated with steroid hormones and growth factors PMID: 12362977 equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate PMID: 12719131 In dilute solutions, several active prostatic acid phosphatase species exist, which are involved in concentration-dependent dissociation/association equilibria PMID: 12962324 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 protein binding with Con A in seminal plasma PMID: 14690244 Transcriptional activation of the prostatic acid phosphatase gene by NF-kappaB in human prostate cancer cells. PMID: 15240830 Prostatic acid phosphatase inactivates lysophosphatidic acid in seminal plasma. PMID: 15280042 analysis of prostatic acid phosphatase binding PMID: 15578709 the GAAAATATGATA-like elements are involved in the transcriptional regulation of hPAP promoter constructs in prostatic cells. PMID: 15985366 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 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 PAP (133-152) and PAP (173-192) were immunogenic and processed from whole PAP in HLA-DRB11501 tg mice. These peptides were capable of stimulating CD4 T lymphocytes from HLA-DRB11501-positive patients with granulomatous prostatitis and normal donors. PMID: 17455230 Prostatic acid phosphatase is not a prostate specific target PMID: 17638863 Suppresses pain by functioning as an ecto-5'-nucleotidase, activating A1-adenosine receptors in the dorsal spinal cord. PMID: 18940592 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 Prostatic acid phosphatase boosts the infectivity of xenotropic murine leukemia virus-related virus. PMID: 19403677 Report safety and immunological efficacy of a DNA vaccine encoding prostatic acid phosphatase in patients with stage D0 prostate cancer. PMID: 19636017 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.

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