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anti-Human ACPP Antibodies:
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Human Polyclonal ACPP Primary Antibody for IHC, IHC (p) - ABIN4347795
Kato, Nicholson, Neiman, Rantalainen, Holmes, Barrett, Uhlén, Nilsson, Spector, Schwenk: Variance decomposition of protein profiles from antibody arrays using a longitudinal twin model. in Proteome science 2011
Show all 2 Pubmed References
Human Polyclonal ACPP Primary Antibody for IHC (p), WB - ABIN513082
Cotella, Hernandez-Enriquez, Duan, Wu, Gazula, Brown, Kaczmarek, Sesti: An evolutionarily conserved mode of modulation of Shaw-like K? channels. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2013
Human Polyclonal ACPP Primary Antibody for ELISA, WB - ABIN570986
Nousiainen, Quintero, Myöhänen, Voikar, Mijatovic, Segerstråle, Herrala, Kulesskaya, Pulkka, Kivinummi, Abo-Ramadan, Taira, Piepponen, Rauvala, Vihko: Mice deficient in transmembrane prostatic acid phosphatase display increased GABAergic transmission and neurological alterations. in PLoS ONE 2014
Human Polyclonal ACPP Primary Antibody for ELISA, IHC - ABIN4347794
Münch, Rücker, Ständker, Adermann, Goffinet, Schindler, Wildum, Chinnadurai, Rajan, Specht, Giménez-Gallego, Sánchez, Fowler, Koulov, Kelly, Mothes, Grivel, Margolis, Keppler, Forssmann, Kirchhoff: Semen-derived amyloid fibrils drastically enhance HIV infection. in Cell 2007
Human Polyclonal ACPP Primary Antibody for ELISA, IHC - ABIN4347792
Quintero, Araujo, Pulkka, Wirkkala, Herrala, Eskelinen, Jokitalo, Hellström, Tuominen, Hirvikoski, Vihko: Prostatic acid phosphatase is not a prostate specific target. in Cancer research 2007
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.
Thirteen single nucleotide polymorphism (SNPs) in acid phosphatase prostate (ACPP) were suggested as candidate causal alleles that underlie ACPP regulation and expression.
we have measured the intramolecular diffusion of the full length and 8-residue deletion peptides at two different pHs (show PCBD1 Antibodies) and found a correlation with fibrillization lag (show STMN1 Antibodies) 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.
Prostatic acid phosphatase delays prostate cancer cell growth in G1 phase of the cell cycle.
Studies suggest that understanding of prostatic acid phosphatase function and regulation of expression will have a significant impact on understanding prostate cancer (PCa (show FLVCR1 Antibodies)) progression and therapy.
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.
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.
Data indicate that hypoxia regulates prostatic acid phosphatase (PAP) through hypoxia-inducible factor 2 alpha (show EPAS1 Antibodies) (HIF2alpha (show EPAS1 Antibodies)) and from stimulated A2B (show ADORA2B Antibodies) adenosine receptors.
GCNT1 (show GCNT1 Antibodies) is over-expressed in prostate cancer and is associated with higher levels of core 2 O-sLe(x) in PSA (show PLAG1 Antibodies), PAP (show REG3A Antibodies) and MUC1 (show MUC1 Antibodies) proteins.
Data indicate that prostate acid phosphatase-based peptide vaccine PAP (show REG3A Antibodies)-114-128 peptide appears to be a relevant for the treatment of prostate cancer.
PAP (show ASAP1 Antibodies)-immunoreactivity was present in type I and one of type III taste cells of taste buds. Thus, it is suggested that PAP (show ASAP1 Antibodies) might be a responsible ectoenzyme for metabolism of extracellular nucleotides, being involved in the regulation of taste signaling in taste buds.
These findings demonstrate that PAP (show ASAP1 Antibodies) secreted by PCa (show ENPP1 Antibodies) cells in OB bone metastases increases osteoprotegerin (show TNFRSF11B Antibodies) and plays a critical role in the vicious cross talk between cancer and bone cells.
functional PAP (show ASAP1 Antibodies)(thorn) neurons are essential for the analgesic effect, which is mediated by NGF (show NGFB Antibodies)-trkA (show NTRK1 Antibodies) signaling.
TMPAP is involved in the control of GABAergic tone in the brain also through exocytosis, and that PAP (show ASAP1 Antibodies) deficiency produces a distinct neurological phenotype.
In male mouse saliva (show RAG1AP1 Antibodies) prostatic acid phosphatase regulates salivation.
Data indicate that prostate acid phosphatase-based peptide vaccine PAP (show ASAP1 Antibodies)-114-128 peptide appears to be a relevant for the treatment of prostate cancer.
this PAP (show ASAP1 Antibodies)-/- mouse model shows that TMPAP is required for the normal function of prostate in mice, and its deficiency leads to prostate adenocarcinoma.
Both prostatic acid phosphatase and ecto-5'-nucleotidase generate adenosine in the dorsal spinal cord.
Prostatic acid phosphatase is required for the antinociceptive effects of thiamine and benfotiamine.
Experiments indicate that PAP (show ASAP1 Antibodies) and NT5E (show NT5E Antibodies) are the main ectonucleotidases that generate adenosine in nociceptive circuits and indicate these enzymes transform pulsatile or sustained nucleotide release into an inhibitory adenosinergic signal.
The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP (show PDAP1 Antibodies). The determined sequence of a 354 bp nucleotide fragment showed 90% identity with the corresponding sequence of human PAP (show PDAP1 Antibodies).
This gene encodes a multidomain protein containing an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology (PH) domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal Src homology 3 (SH3) domain. The protein localizes in the Golgi apparatus and at the plasma membrane, where it colocalizes with protein tyrosine kinase 2-beta (PYK2). The encoded protein forms a stable complex with PYK2 in vivo. This interaction appears to be mediated by binding of its SH3 domain to the C-terminal proline-rich domain of PYK2. The encoded protein is tyrosine phosphorylated by activated PYK2. It has catalytic activity for class I and II ArfGAPs in vitro, and can bind the class III Arf ARF6 without immediate GAP activity. The encoded protein is believed to function as an ARF GAP that controls ARF-mediated vesicle budding when recruited to Golgi membranes. In addition, it functions as a substrate and downstream target for PYK2 and SRC, a pathway that may be involved in the regulation of vesicular transport. Multiple transcript variants encoding different isoforms have been found for this gene.
, prostatic acid phosphatase
, prostatic acid phosphotase
, thiamine monophosphatase
, PYK2 C terminus-associated protein
, arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
, centaurin, beta 3
, development and differentiation enhancing factor 2
, development and differentiation-enhancing factor 2
, paxillin-associated protein with ARF GAP activity 3
, pyk2 C-terminus-associated protein
, fluoride-resistant acid phosphatase
, lysosomal acid phosphatase
, prostatic acid phosphatase (rPAP)
, acid phosphatase, prostate
, tyrosine acid phosphatase
, prostatic acid phosphatase-like
, testicular acid phosphatase homolog