Protein RER1 (RER1), Chicken, ELISA Kit
- Known as:
- Protein RER1 (RER1), Chicken, Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- G4009
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- Glory
- Gene target:
- Protein RER1 (RER1) Chicken ELISA Kit
Related genes to: Protein RER1 (RER1), Chicken, ELISA Kit
- Gene:
- RER1 NIH gene
- Name:
- retention in endoplasmic reticulum sorting receptor 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1p36.32
- Locus Type:
- gene with protein product
- Date approved:
- 2004-12-17
- Date modifiied:
- 2016-10-05
Related products to: Protein RER1 (RER1), Chicken, ELISA Kit
Related articles to: Protein RER1 (RER1), Chicken, ELISA Kit
- Gene expression profiling in neurodegenerative diseases such as Alzheimer’s Disease (AD) is frequently performed using real-time quantitative polymerase chain reaction (RT-qPCR). The accuracy of this technique relies heavily on selecting suitable reference genes (RGs) for normalization and internal control. Ideally, RGs should maintain consistent transcription levels, unaffected by cellular or pathological changes. However, identifying stable RGs is challenging, particularly in diseases like AD, where gene expression fluctuates across disease stages. This study aimed to determine the most stable RGs in two brain regions - cortex (CTX) and hippocampus (HIPP) - of male and female 5XFAD mice, a model of familial AD. The stability of five commonly used RGs namely Gapdh, Ppia, Rer1, Rpl27 and Rps29, was evaluated using GeNorm, NormFinder, BestKeeper, and EndoGene algorithms across three AD stages: prodromal (2 months of age, mo), early (4 mo), and late (7 and 10 mo). Results revealed region-, sex-, and time-dependent differences in RG expression stability, reflecting the distinct vulnerability of CTX and HIPP to Aβ pathology. Using the two most stable RGs for normalization improved precision, reducing variability and increasing the significance level in target gene expression analyses. These findings emphasize the necessity of validating RGs under specific experimental conditions to ensure reliable RT-qPCR quantification in AD research. - Source: PubMed
Publication date: 2026/02/04
Daini EleonoraAntonioni KristyPiemontese MonicaBodria MartinaZoli MicheleVilella Antonietta - A subset of the four-pass transmembrane proteins called C8 tetraspanins (TspanC8) can bind and promote the cell surface localization of ADAM10 (A Disintegrin and Metalloproteinase 10). ADAM10 is a conserved transmembrane metalloprotease essential for metazoan embryonic development and human health. However, the in vivo functional relationships between C8 tetraspanins and ADAM10 are not fully understood. has two paralogous tetraspanins, TSP-12 and TSP-14, that resemble the mammalian TspanC8 proteins. We have previously shown that TSP-12/TspanC8 can bind SUP-17/ADAM10 and promote its cell surface localization in early embryos. In this study, we identified the specific step in the secretory pathway where TSP-12-SUP-17 interaction is needed. We found that TSP-12 and SUP-17 share a mutually dependent, yet cell type- and developmental stage-specific relationship in their Golgi trafficking itinerary. In the early embryo, TSP-12 and SUP-17 depend on each other for their transit through the Golgi. However, only SUP-17 is required for proper Golgi trafficking of TSP-12 in the developing oocytes. We further showed that the ER accumulation of SUP-17 in embryos lacking TSP-12 is mediated by the Retention in Endoplasmic Reticulum 1 protein RER-1. These findings, combined with our previous work showing that TSP-12 and TSP-14 function redundantly in endosomes for the recycling of the type II receptor of the BMP signaling pathway, showcase the dynamic and versatile functions of TSP-12 in membrane trafficking in specific cellular contexts. They further highlight the importance of dissecting the functional relationships between TspanC8 proteins and ADAM10 in vivo. - Source: PubMed
Publication date: 2026/01/02
Liu ZhiyuWilliams ByronWang LinClark Frances KVignogna Ryan CFromme J ChristopherLiu Jun - Plants have a crucial role in providing essential amino acids for human nutrition. Nine of the 20 proteinogenic amino acids are exclusively synthesized de novo in plastids, yet transporters mediating their exchange across the plastid inner envelope remain unknown. Here we identify RETICULATA1 (RE1) as a plastid-localized transporter for basic amino acids-including Arg, Citr, Orn and Lys-in Arabidopsis thaliana. Loss-of-function mutants display a reticulate leaf phenotype, contain lower amounts of basic amino acids and are impaired in amino acid homeostasis. RE1 belongs to a novel class of membrane transport proteins that contain a domain of unknown function 3411 and are found exclusively in plastid-containing organisms. Our results indicate functional overlap with its closest homologue RER1, as the double mutant is lethal. Isotope labelling reveals that loss of RE1 reduces basic amino acid biosynthesis and affects the equilibration of plastidic and cytosolic amino acid pools. These findings uncover a critical role for plastidial amino acid transporters in coordinating primary metabolism, development and nutrient allocation in plants. - Source: PubMed
Publication date: 2025/08/22
Kuhnert FranziskaWesthoff PhilippValencia VanessaKrüger StephanVogel KarolinaLundquist Peter KRosar ChristianGoss TatjanaWeber Andreas P M - Retention in endoplasmic reticulum sorting receptor 1 (RER1) mediates the retention and retrieval of select cargo proteins, and thereby regulates protein transport in the secretory pathway and assembly of distinct protein complexes. Recently, RER1 was implicated in the assembly and subcellular transport of the TREM2-DAP12 immune receptor complex, and its function in intracellular signaling and phagocytosis. However, the role of RER1 in the regulation of immune cell metabolism remained unknown. Here, we demonstrate an important role of RER1 in the lipid metabolism of monocytic and macrophage-like differentiated THP-1 cells. The deficiency of RER1 resulted in the accumulation of lipid droplets (LDs) in both monocytes and macrophage-like cells. Comprehensive mass spectrometry analyses revealed complex changes in the cellular lipid metabolism and the composition of LDs. RNA sequencing revealed an important role of RER1 in the regulation of genes related to lipid metabolism. Further, western immunoblotting confirmed an important role of RER1 in the expression of select key proteins involved in cellular lipid metabolism. The combined data indicate that RER1 plays an essential role in lipid metabolism in monocytes and macrophages. - Source: PubMed
Publication date: 2025/08/13
Liu YanxiaTheil SandraYaghmour Mohamed HKerksiek AnjaChen PengSchmidt-Wolf Ingo G HBarker RebeccaBartok EvaLütjohann DieterThiele ChristophWalter Jochen - Proper normalization of gene expression data is essential for detecting early molecular alterations in eye disorders. In this study, we assessed seven potential reference genes (18S, RER1, ACTB, GAPDH, PGK1, UBC, and AP3D1) in tear fluid collected from individuals with dry eye disease and glaucoma patients using benzalkonium-preserved topical medications, as well as from healthy controls. Utilizing various stability analysis methods (geNorm, NormFinder, comparative ∆CT method, BestKeeper, and RefFinder), we determined that 18S, RER1, and ACTB were the most stable reference genes, while UBC and AP3D1 displayed significant variability. To confirm these results, we evaluated the inflammasome-associated genes ASC and Caspase-1, which showed marked upregulation in patients' tear fluid when normalized with the top-rated reference genes. This finding emphasizes the critical nature of selecting robust reference genes. Our research underscores the significance of rigorous validation in studies involving tear fluid to ensure accurate gene expression results, thereby assisting in identifying clinically relevant biomarkers for ocular surface diseases. Implementing well-validated normalization methods will likely enhance sensitivity and specificity in recognizing early pathological developments in ocular surface conditions like dry eye disease or the toxicity associated with benzalkonium chloride-containing glaucoma medications. - Source: PubMed
Publication date: 2025/07/09
Ojeda Diego AAhmadzadeh HoomanOrgul SarpBedoya Angela GomezGupta SwatiHeld KatherineSwaminathan Swarup SSabater Alfonso L