ALPP Antibody (OASA09105)
- Known as:
- ALPP Antibody (OASA09105)
- Catalog number:
- oasa09105
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ALPP Antibody (OASA09105)
Ask about this productRelated genes to: ALPP Antibody (OASA09105)
- Gene:
- ALPG NIH gene
- Name:
- alkaline phosphatase, germ cell
- Previous symbol:
- ALPPL2
- Synonyms:
- GCAP
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 1990-07-06
- Date modifiied:
- 2018-04-16
- Gene:
- ALPP NIH gene
- Name:
- alkaline phosphatase, placental
- Previous symbol:
- -
- Synonyms:
- PALP, PLAP
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2018-02-28
Related products to: ALPP Antibody (OASA09105)
Related articles to: ALPP Antibody (OASA09105)
- Epigenetic modifications have been linked to atherosclerotic cardiovascular disease and could constitute therapeutic targets. - Source: PubMed
Publication date: 2026/06/03
Ingold MarkusMüller CelineKrolevets MykhailoYapıcı ElifRapp SteffenSchuster Alexander KTesarz JonasHeinrich IsabelWeinmann-Menke JuliaStrauch KonstantinLackner Karl JKonstantinides StavrosRuf WolframAndrade-Navarro Miguel ANiehrs ChristofGori TommasoLurz PhilippWild Philipp STen Cate Vincent - Human naive pluripotent stem cells established from the epiblasts of preimplantation blastocysts provide a useful model for mechanistic studies of pluripotency regulation and lineage differentiation. Important advances have been made to optimize culture conditions and define molecular criteria for naive pluripotency. However, the identity of naive-specific surface markers and the underlying molecular mechanism of naive pluripotency regulation remain poorly understood. Here, we identify alkaline phosphatase placental-like 2 (ALPPL2) as a prominent naive-specific surface marker by systematic proteomic and transcriptomic analyses. Furthermore, we demonstrate that ALPPL2 is essential for both the establishment and maintenance of naive pluripotency. Moreover, we show that ALPPL2 can interact with the RNA-binding protein IGF2BP1 to stabilize the mRNA levels of the naive pluripotency transcription factors TFCP2L1 and STAT3 to regulate naive pluripotency. Overall, our study identifies a functional surface marker for human naive pluripotency, providing a powerful tool for human-naive-pluripotency-related mechanistic studies. - Source: PubMed
Bi YanTu ZhifenZhang YanpingYang PengGuo MingyueZhu XuehaoZhao ChengchenZhou JianfengWang HongWang YixuanGao Shaorong - Alkaline phosphatase placental-like 2 (ALPPL2) is a member of the ALPP alkaline phosphatase family and is reported to be associated with the growth of some tumors. Gastric cancer is one of the most common cancers worldwide. We previously identified a distinct expression pattern of ALPPL2 between gastric cancer and adjacent normal tissues. In this study, we examined the expression of ALPPL2 in gastric adenocarcinoma and its ability to predict prognosis. We used bioinformatics analysis and immunohistochemistry to examine the expression pattern of ALPPL2 and analyzed the associations between ALPPL2 level and perioperative characteristics and the prognosis of gastric adenocarcinoma patients by Kaplan-Meier plotter analysis. Our results indicated that the expression of ALPPL2 was significantly increased in gastric adenocarcinoma (P < .01) and was an independent factor (P < .05) that could provide reliable prognostic information on gastric adenocarcinoma patients. High expression of ALPPL2 was associated with advanced TNM stage (P < .05) and high HER-2 expression (P < .01). Our study suggests that ALPPL2 has the potential to reveal prognostic information on gastric cancer. - Source: PubMed
Publication date: 2018/11/26
Liu ShuangMao QinshengXue WanjiangZhang XiaojingQi YueWang YingjingChen PeiZhou Qing - Nucleoside analogues are the most promising drugs for the treatment of pancreatic cancer to date. However, their use is often limited due to toxic side effects. Aptamer-mediated targeted delivery of these drugs to cancer cells could maximize their effectiveness and concomitantly minimize the toxic side effects by reducing uptake into normal cells. Previously, we identified a pancreatic cancer-specific, nuclease-resistant RNA aptamer, SQ2, which binds to alkaline phosphatase placental-like 2 (ALPPL2), a putative biomarker for pancreatic cancer. In this study, we demonstrate that the aptamer can be internalized into pancreatic cancer cells and can thus be used for the targeted delivery of therapeutics. Using the aptamer as a ligand, we established that glycophosphatidylinositol-anchored ALPPL2 is internalized by the cells through clathrin-independent and caveolae-dependent or dynamin-mediated cell-type-dependent pathways. Finally, we show that SQ2 can deliver nucleoside drug 5-fluoro-2'-deoxyuridine specifically to ALPPL2-expressing pancreatic cancer cells, inhibiting cell proliferation. - Source: PubMed
Publication date: 2015/04/28
Dua PoojaS SajeeshKim SoyounLee Dong-ki - Exon splicing enhancers (ESEs) overlap with amino acid coding sequences implying a dual evolutionary selective pressure. In this study, we map ESEs in the placental alkaline phosphatase gene (ALPP), absent in the corresponding exon of the ancestral tissue-non-specific alkaline phosphatase gene (ALPL). The ESEs are associated with amino acid differences between the transcripts in an area otherwise conserved. We switched out the ALPP ESEs sequences with the sequence from the related ALPL, introducing the associated amino acid changes. The resulting enzymes, produced by cDNA expression, showed different kinetic characteristics than ALPL and ALPP. In the organism, this enzyme will never be subjected to selection because gene splicing analysis shows exon skipping due to loss of the ESE. Our data prove that ESEs restrict the evolution of enzymatic activity. Thus, suboptimal proteins may exist in scenarios when coding nucleotide changes and consequent amino acid variation cannot be reconciled with the splicing function. - Source: PubMed
Publication date: 2014/04/01
Falanga AlessiaStojanović OzrenKiffer-Moreira TinaPinto SofiaMillán José LuisVlahoviček KristianBaralle Marco