APPL1 antibody
- Known as:
- APPL1 (anti-)
- Catalog number:
- orb10121
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- APPL1 antibody
Related genes to: APPL1 antibody
- Gene:
- APPL1 NIH gene
- Name:
- adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1
- Previous symbol:
- -
- Synonyms:
- APPL
- Chromosome:
- 3p14.3
- Locus Type:
- gene with protein product
- Date approved:
- 2007-01-26
- Date modifiied:
- 2016-03-14
Related products to: APPL1 antibody
Related articles to: APPL1 antibody
- Gastrointestinal (GI) involvement in systemic sclerosis (SSc) affects up to 90% of patients and is a major driver of morbidity and mortality. Despite its clinical importance, GI disease in SSc is highly heterogeneous, with upper and lower GI manifestations representing distinct phenotypic extremes whose underlying immunologic basis remains poorly defined. - Source: PubMed
Publication date: 2026/05/21
McMahan Zsuzsanna HPuttapaka SrinivasHulett TylerShah Ami AFaheem KathrynHu ShaohuiSonmez GamzeRamos PedroKulkarni Subhash - Here we investigate the status of the adiponectin-PEPITEM pathway in early, treatment naive rheumatoid arthritis (RA) and psoriatic arthritis (PsA) and the therapeutic efficacy of PEPITEM administration in preclinical models. - Source: PubMed
Publication date: 2026/04/13
Wahid MussaratKemble SamuelAbudu OladimejiSaviano AnellaMahony ChristopherLewis Jonathan WNicholson Thomas ASchettino AnnaMarigliano NoemiFrost KathrynBegum JenefaUrbanowski Alyssa MLimo MarionJha RakeshJarquin Sandra MartinezPezhman LalehDegan Abbie E AAnderson Amy ESmith Charlotte GBatki ArmaitiAdams HollyCaso FrancescoScarpa RaffaeleMcInnes IainSiebert StefanPratt Arthur GFiler AndrewRaza KarimCroft Adam PChimen Myriamde Cogan FelicityRainger G EdIqbal Asif JMaione FrancescoMcGettrick Helen M - - Source: PubMed
Cellular Longevity Oxidative Medicine And - Adiponectin and irisin regulate energy homeostasis and interact with peroxisome proliferator-activated receptor coactivator 1α (PGC-1α). However, whether they establish a signal connection via PGC-1α is unclear. In the current study, the expression of irisin was significantly decreased in the skeletal muscle of adiponectin knockout (KO) mice, accompanied by a de crease in APPL1/p38 mitogen-activated protein kinase (MAPK)/PGC-1α. However, adiponectin administration reversed this effect. In vitro, the p38 MAPK/PGC-1α signalling pathway mediated adiponectin-induced FNDC5 expression and irisin release in mouse-derived C2C12 myotube cells. Moreover, obesity caused dysregulation of the adiponectin/APPL1/p38 MAPK/PGC-1α signalling pathway in murine skeletal muscle, ultimately inhibiting irisin synthesis and secretion; meanwhile, prolonged exercise or exogenous recombinant adiponectin intervention activated this pathway in mouse skeletal muscle. This corresponded with an apparent improvement in high-fat diet-induced insulin resistance. The effect of mechanically stretching C2C12 myotube cells was consistent with in vivo findings. Hence, adiponectin upregulates irisin through the APPL1/p38MAPK/PGC-1α signalling pathway in murine skeletal muscle, which may enhance insulin sensitivity. - Source: PubMed
Publication date: 2026/02/05
Huang RuiqiXu SitongGuo QiCao ShichengTang DonghuiYi Xuejie - Myosin VI (MYO6) is the only actin-based motor protein that moves toward the minus end of actin filaments. It participates in multiple cellular processes, including endocytosis, secretion, autophagy, and the formation of apical stereocilia and microvilli in highly specialized epithelia. These diverse functions are mediated by specific cargo-adaptor proteins that recruit MYO6 to distinct cellular compartments. We have previously demonstrated that loss of MYO6 function in Snell's waltzer mice leads to several defects during spermatogenesis, resulting in reduced male fertility. Here, we show for the first time that MYO6 and selected binding partners are differentially expressed in mouse epididymal epithelium, a highly specialized mammalian epithelia developing apical microvilli. Using immunocytochemistry, confocal microscopy, and biochemical approaches we found that: (i) MYO6 is present in the epithelium of the common efferent duct and all segments of the epididymis, (ii) MYO6 and Dab2 colocalize predominantly at the apical surface of epithelial cells in the efferent duct and caput, (iii) MYO6 and GIPC1 are mainly detected in epithelial cells in the caput and corpus, with the lowest level observed in the cauda. Moreover, depletion of MYO6 results in altered distribution of clathrin and APPL1 in epididymal epithelial cells and causes ultrastructural abnormalities. Altogether, our findings indicate that MYO6 contributes to the endocytic pathway in the mouse epididymal epithelium, a process essential for generating the microenvironment required for sperm maturation. In addition, MYO6 supports the structural organization of apical microvilli, thereby facilitating sperm transport through the epididymal duct. - Source: PubMed
Richert AnnaLenartowski RobertWasąg PiotrZakrzewski PrzemysławSuszyńska-Zajczyk JoannaKaratsai-Miaskowska OlenaRędowicz Maria JolantaLenartowska Marta