PPAPDC2 Blocking Peptide
- Known as:
- PPAPDC2 Blocking Peptide
- Catalog number:
- 33r-6306
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- PPAPDC2 Blocking Peptide
Related genes to: PPAPDC2 Blocking Peptide
- Gene:
- PLPP6 NIH gene
- Name:
- phospholipid phosphatase 6
- Previous symbol:
- PPAPDC2
- Synonyms:
- FLJ90191, FLJ46512, PDP1
- Chromosome:
- 9p24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-15
- Date modifiied:
- 2016-10-05
Related products to: PPAPDC2 Blocking Peptide
Related articles to: PPAPDC2 Blocking Peptide
- Previous genomic efforts on chromosome 9p deletion and duplication syndromes have utilized low-resolution strategies (i.e., karyotypes, chromosome microarrays). These studies have provided important initial insights into these syndromes. This current study is the first large-scale whole-genome sequencing (WGS) study of 100 individuals from families with chromosome 9p syndromes. - Source: PubMed
Publication date: 2025/10/24
Wang YingxiSams Eleanor ISlaugh RachelCrocker SandraHurtado Emily CordovaTracy SophiaHou Ying-Chen ClaireMarkovic ChristopherValle KostandinTate VictoriaBelhassan KhadijaAppelbaum ElizabethAkinwe TitilopeStarosta Rodrigo TCao YangNeilson AmberLiu YuJensen NathanielGhasemi RezaLindsay TinaManuel JuanaCouteranis SophiaKremitzki MilinnUstanik JackAntonacci ThomasNg Jeffrey KEmory AndrewMetz LauraDeLuca TracieLyons Katherine NSinnwell ToniThomeczek BrianneWang KymmeSisneros NickMuraleedharan MeghaKethireddy AnanthaCorbo MarcoGowda HarshaKing Katherine AGurnett Christina ADutcher Susan KGooch CatherineLi Yang EMitchell Matthew WPeterson Kevin AHorani AmjadRosenfeld Jill ABi WeiminStankiewicz PawelChao Hsiao-TuanPosey Jennifer EGrochowski Christopher MDardas ZainPuffenberger Erik GPearson Christopher EKooy FrankAnnear DaleInnes A MicheilHeinz MichaelHead RichardFulton RobertToutain Stephan Antonacci-Fulton LucindaCui XiaoxiaMitra Robi DCole F SessionsNeidich JulieDickson Patricia IMilbrandt JeffreyTurner Tychele N - Previous genomic efforts on chromosome 9p deletion and duplication syndromes have utilized low resolution strategies (i.e., karyotypes, chromosome microarrays). We present the first large-scale whole-genome sequencing (WGS) study of 100 individuals from families with 9p-related syndromes including 85 unrelated probands through the 9P-ARCH (dvanced esearch in hromosomal ealth: Genomic, Phenotypic, and Functional Aspects of -Related syndromes) research network. We analyzed the genomic architecture of these syndromes, highlighting fundamental features and their commonalities and differences across individuals. This work includes a machine-learning model that predicts 9p deletion syndrome from gene copy number estimates using WGS data. Two Late Replicating Regions (LRR1 [a previously un-named human fragile site], LRR2) were identified that contain most structural variant breakpoints in 9p deletion syndrome pointing to replication-based issues in structural variant formation. Furthermore, we show the utility of using WGS information to obtain a comprehensive understanding of 9p-related variation in an individual with complex structural variation where chromothripsis is the likely mechanism. Genes on 9p were prioritized based on statistical assessment of human genomic variation. Furthermore, through application of spatial transcriptomics to embryonic mouse tissue we examined 9p-gene expression in craniofacial and brain development. Through these strategies, we identified 24 important genes for the majority (83%) of individuals with 9p deletion syndrome including , , , , , , , and . Two genes (, ) are involved in mitochondrial function and testing of the mitochondrial genome revealed excess copy number in individuals with 9p deletion syndrome. This study presents the most comprehensive genomic analysis of 9p-related syndromes to date, with plans for further expansion through our 9P-ARCH research network. - Source: PubMed
Publication date: 2025/03/30
Wang YingxiSams Eleanor ISlaugh RachelCrocker SandraHurtado Emily CordovaTracy SophiaHou Ying-Chen ClaireMarkovic ChristopherValle KostandinTate VictoriaBelhassan KhadijaAppelbaum ElizabethAkinwe TitilopeTzovenos Rodrigo StarostaCao YangNeilson AmberLiu YuJensen NathanielGhasemi RezaLindsay TinaManuel JuanaCouteranis SophiaKremitzki MilinnUstanik JackAntonacci ThomasNg Jeffrey KEmory AndrewMetz LauraDeLuca TracieLyons Katherine NSinnwell ToniThomeczek BrianneWang KymmeSisneros NickMuraleedharan MeghaKethireddy AnanthaCorbo MarcoGowda HarshaKing KatherineGurnett Christina ADutcher Susan KGooch CatherineLi Yang EMitchell Matthew WPeterson Kevin AHorani AmjadRosenfeld Jill ABi WeiminStankiewicz PawelChao Hsiao-TuanPosey JenniferGrochowski Christopher MDardas ZainPuffenberger ErikPearson Christopher EKooy FrankAnnear DaleInnes A MicheilHeinz MichaelHead RichardFulton RobertToutain Stephan Antonacci-Fulton LucindaCui XiaoxiaMitra Robi DCole F SessionsNeidich JulieDickson Patricia IMilbrandt JeffreyTurner Tychele N - Lipid phosphate phosphatases are a family of enzymes with diverse cellular metabolic functions. Phospholipid phosphatase 6 (PLPP6) is a regulator of cellular polyisoprenyl phosphates; however, its functions remain to be determined. Here, mouse PLPP6 was characterized to possess similar catalytic properties as the human enzyme. knockout mice ( ) were generated and displayed decreased airway allergen sensitization, pointing to a role for PLPP6 in the early events of lung allergic responses. Dendritic cell (DC) responses were investigated and endocytosis of allergen via macropinocytosis was decreased in DCs that had lower cholesterol content. When reversed by cholesterol loading, the DC macropinocytosis defect is corrected. Adoptive transfer of DCs to wild-type mice during sensitization was sufficient to decrease allergen-induced responses Together, our findings have identified PLPP6 as a pivotal regulator of DC cholesterol content and macropinocytosis, cellular mechanisms that are important for pathologic responses in allergen-induced lung inflammation. - Source: PubMed
Publication date: 2022/09/23
Brüggemann Thayse RCarlo TroyKrishnamoorthy NandiniDuvall Melody GAbdulnour Raja-Elie ENijmeh JuliePeh Hong YongFilippakis HarilaosCroze Roxanne HGoh ByoungsookOh Sungwhan FLevy Bruce D - Equine melanocytic neoplasm (EMN) is a cutaneous neoplasm and is mostly observed in aged grey horses. This preliminary study aimed to identify potential proteins to differentiate normal, mild and severe EMN from serum proteomic profiling. Serum samples were collected from 25 grey horses assigned to three groups: normal (free of EMN; = 10), mild ( = 6) and severe EMN ( = 9). To explore the differences in proteins between groups, proteomic profiling and analysis were employed. Accordingly, 8241 annotated proteins out of 8725 total proteins were compared between normal and EMN groups and inspected based on differentially expressed proteins (DEPs). Through DEP analysis, 95 significant DEPs differed between normal and EMN groups. Among these DEPs, 41 significant proteins were categorised according to protein functions. Based on 41 significant proteins, 10 were involved in metabolism and 31 in non-metabolism. Interestingly, phospholipid phosphatase6 (PLPP6) and ATPase subunit alpha (Na+/K+-ATPase) were considered as potential proteins uniquely expressed in mild EMN and related to lipid and energy metabolism, respectively. Non-metabolism-related proteins (BRCA1, phosphorylase B kinase regulatory subunit: PHKA1, tyrosine-protein kinase receptor: ALK and rho-associated protein kinase: ROCK1) correlated to melanoma development differed among all groups. The results of our study provide a foundation for early EMN biomonitoring and prevention. - Source: PubMed
Publication date: 2021/06/27
Tesena ParichartKingkaw AmornthepVongsangnak WanwipaPitikarn SurakietPhaonakrop NarumonRoytrakul SittirukKovitvadhi Attawit