MON1A
- Known as:
- MON1A
- Catalog number:
- Y214457
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- MON1A
Related genes to: MON1A
- Gene:
- MON1A NIH gene
- Name:
- MON1 homolog A, secretory trafficking associated
- Previous symbol:
- -
- Synonyms:
- MGC13272, SAND1
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2005-03-02
- Date modifiied:
- 2018-06-04
Related products to: MON1A
Anti-Mon1a/SAND1 Polyclonal Antibody (OAAI00790)Antibodies: MON1A (aa478-489) HOST: Goat Clonality: pAbAntibodies: MON1A (aa589-601) HOST: Goat Clonality: pAbBos taurus,Bovine,MON1A,Vacuolar fusion protein MON1 homolog ABovine MON1 homolog A (yeast) (MON1A) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitBovine Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitBovine Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kit SpeciesBovineCanine Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitCanine Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitChicken MON1 homolog A (yeast) (MON1A) ELISA kit, Species Chicken, Sample Type serum, plasmaChicken Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitChicken Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kitChicken Vacuolar fusion protein MON1 homolog A(MON1A) ELISA kit SpeciesChickenChicken,Gallus gallus,MON1A,RCJMB04_26e14,Vacuolar fusion protein MON1 homolog A Related articles to: MON1A
- Red blood cells (RBCs) transport oxygen but accumulate oxidative damage over time, reducing function in vivo and during storage, critical for transfusions. To explore the genetics of RBC resilience, we profiled proteins, metabolites, and lipids from fresh and stored RBCs from 350 genetically diverse mice. Our analysis identified over 6,000 quantitative trait loci (QTLs). Compared to other tissues, the prevalence of trans genetic effects over cis ones reflects the absence of de novo protein synthesis in anucleated RBCs. QTL hotspots at Hbb, Hba, Mon1a, and (storage-specific) Steap3 linked ferroptosis to hemolysis. Proteasome QTLs clustered at multiple loci, underscoring the importance of degrading oxidized proteins. Post-translational modification (PTM) QTLs mapped predominantly to hemoglobins, including cysteine residues. The loss of reactive C93 in humanized mice (hemoglobulin beta [HBB] C93A) disrupted redox balance, glutathione pools, glutathionylation, and redox PTMs. These findings highlight genetic regulation of RBC oxidation, with implications for transfusion biology and oxidative-stress-dependent hemolytic disorders. - Source: PubMed
Publication date: 2025/11/19
Keele Gregory RDzieciatkowska MonikaHay Ariel MVincent MatthewO'Connor CallanStephenson DanielReisz Julie ANemkov TravisHansen Kirk CPage Grier PZimring James CChurchill Gary AD'Alessandro Angelo - Autophagy is a fundamental cellular process, conserved across species from yeast to mammals, that plays a crucial role in maintaining cellular homeostasis. The functionally conserved MON1-CCZ1 (MC1) complex serves as a guanine nucleotide exchange factor (GEF) for the RAB GTPase RAB7A and is indispensable for directing RAB7A recruitment to autophagosome or lysosomal membranes. Despite its critical role, the precise molecular mechanism underlying the assembly of the human MON1A-CCZ1 (HsMC1) complex and its specific GEF activity towards RAB7A has remained unclear. In this study, we report the high-resolution cryo-electron microscopy (cryo-EM) structure of the HsMC1 GEF domain in a complex with the nucleotide-free RAB7A at 2.85 Å resolution. Our structural data demonstrate that engagement with the HsMC1 complex induces marked conformational shifts in the phosphate-binding loop (P-loop) and Switch I/II regions of RAB7A. A striking feature of this complex is the direct interaction between the P-loop of RAB7A and CCZ1, a structural detail not previously observed. Furthermore, biochemical assays targeting residues within Interface I or II of the HsMC1-RAB7A complex highlight their critical role in mediating the interaction and suggest a unique mechanism for nucleotide exchange facilitated by the HsMC1 complex. These findings provide novel molecular insights into the functional mechanisms of the HsMC1-RAB7A complex, offering a robust structural framework to inform future investigations into disease-related targets and therapeutic development. - Source: PubMed
Publication date: 2025/05/26
Li XinnaLi DanTang DanHuang XiaofangBao HuiWang JiaweiQi Shiqian - Next-generation sequencing has enabled precision therapeutic approaches that have improved the lives of children with rare diseases. Congenital diarrhea and enteropathies (CODEs) are associated with high morbidity and mortality. Although treatment of these disorders is largely supportive, emerging targeted therapies based on genetic diagnoses include specific diets, pharmacologic treatments, and surgical interventions. - Source: PubMed
Gaibee ZeenatWarner NeilBugda Gwilt KatlynnLi WenjuanGuan ReiYourshaw MichaelWhittaker Hawkins RyderZorbas ChristianeSt-Germain JonathanTabatabaie MahdiMao SuliPinsk VeredYerushalmi BaruchWang Lee-KaiNelson Stanley FWozniak LauraShouval Dror SMatar ManarAssa AmitFrost NathanielJimenez LissetteAcra SariWalters ThomasMouat StephenLi MichaelLafontaine Denis L JTyska MatthewRaught BrianAvitzur YaronLencer Wayne IGoldenring James RMartín Martín GThiagarajah Jay RMuise Aleixo M - Red blood cells (RBCs) transport oxygen but accumulate oxidative damage over time, reducing function in vivo and during storage-critical for transfusions. To explore genetic influences on RBC resilience, we profiled proteins, metabolites, and lipids from fresh and stored RBCs obtained from 350 genetically diverse mice. Our analysis identified over 6,000 quantitative trait loci (QTL). Compared to other tissues, prevalence of genetic effects over reflects the absence of protein synthesis in anucleated RBCs. QTL hotspots at Hbb, Hba, Mon1a, and storage-specific Steap3 linked ferroptosis to hemolysis. Proteasome components clustered at multiple loci, underscoring the importance of degrading oxidized proteins. Post-translational modifications (PTMs) mapped predominantly to hemoglobins, particularly cysteine residues. Loss of reactive C93 in humanized mice (HBB C93A) disrupted redox balance, affecting glutathione pools, protein glutathionylation, and redox PTMs. These findings highlight genetic regulation of RBC oxidation, with implications for transfusion biology and oxidative stress-dependent hemolytic disorders. - Source: PubMed
Publication date: 2025/03/04
Keele Gregory RDzieciatkowska MonikaHay Ariel MVincent MatthewO'Connor CallanStephenson DanielReisz Julie ANemkov TravisHansen Kirk CPage Grier PZimring James CChurchill Gary AD'Alessandro Angelo - - Source: PubMed
Tang YubinHan YaoyaoGuo ZhenpengLi YingGong XinyuZhang YuchaoLiu HaoboZhou XindiXu DaichaoZhang YixiaoPan Lifeng