MNS1 antibody
- Known as:
- MNS1 (anti-)
- Catalog number:
- orb100248
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- MNS1 antibody
Related genes to: MNS1 antibody
- Gene:
- MNS1 NIH gene
- Name:
- meiosis specific nuclear structural 1
- Previous symbol:
- -
- Synonyms:
- FLJ11222, SPATA40
- Chromosome:
- 15q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-20
- Date modifiied:
- 2015-11-23
Related products to: MNS1 antibody
Related articles to: MNS1 antibody
- is a common alternative host to mammalian cell lines for heterologous production of recombinant proteins due to its cost-effectiveness and accelerated development. Its native N-linked glycosylation, however, yields high-mannose structures that differ from those commonly found on secreted recombinant proteins used in biopharmaceuticals. The feasibility of humanizing 's glycosylation pathway has been demonstrated, but routine engineering of this attribute remains underdeveloped. In this study, we reconstructed a humanized glycosylation pathway capable of producing the biantennary GlcNAc2Man3GlcNAc2 (G0) glycan structure. We report a previously undescribed synthetic lethality related to the overexpression of α1-2 mannosidase (MNS1) and the deletion of the native OCH1 gene that can be mitigated by using weaker native promoters for genes modified in the glycosylation pathway. Engineered strains exhibited reduced growth rates compared to unmodified strains, and RNA sequencing revealed upregulated stress response and cell cycle pathways in glycoengineered strains. Through transcriptomics-guided gene knockouts, particularly in the MAPK signaling cascade, we partially restored growth in a G0-engineered strain. This study demonstrates a targeted, host biology-informed strategy for improving glycoengineering in by combining a CRISPR-Cas9 genome-editing system and transcriptomic analysis. - Source: PubMed
Publication date: 2026/07/20
Yang YuchenNaranjo Christopher ADalvie Neil CHinckley Joshua AShi ShutingLove J Christopher - The Xinjiang Black pig is an excellent breed developed by the Xinjiang Production and Construction Corps in the 1990s; however, it has been endangered by the impact of commercial breeds. Whole genomes of 224 individuals from the Xinjiang Black pig conservation population were resequenced. Genetic structure and diversity analyses revealed that Xinjiang Black pigs underwent severe inbreeding and were genetically closely linked to Landrace pigs. The genetic diversity of the F generation was well preserved in the existing breeding scheme. A total of 686 significant selection regions and 406 candidate genes were identified using and θπ complementary methods, with Xinjiang Black pigs, Min pigs, and Laiwu pigs as ancestral populations, and F. Based on Gene Ontology, Kyoto Encyclopedia of Genes and Genomes, and quantitative trait loci annotations, potential germplasm candidate genes were identified. Among these, , , and are associated with fat deposition; , , , and are closely associated with male reproductive ability; and are strongly associated with oestrous cycle regulation and oocyte maturation; and and are extremely important for osmotic regulation and foetal survival. These findings deepen our understanding of the genetic mechanisms of artificial selection in Xinjiang Black pigs and provide a theoretical basis for subsequent breeding and genetic research on this breed. - Source: PubMed
Publication date: 2026/02/28
Tian MingmingFeng YunWang HaitaoWang QiangDong JingyangZhao HaichaoYang FahuiLi MengxunPu GuangZhang XinyinWang DanLi GuangChen HongweiHuang Tao - Leghemoglobin (LegH) is a heme-binding protein and a key ingredient in plant-based meat products, as it imparts the characteristic color and flavor of animal meat. However, achieving high-level secretory expression of LegH in food-grade microbial hosts remains challenging. Here, we applied multistep engineering of the secretory pathway in Kluyveromyces marxianus, a food-safe yeast, to enhance secretion of leghemoglobin A (LBA). A chimeric signal peptide combining the Ost1 signal peptide with the α-factor pro-region enabled efficient secretion of LBA. Further improvements were achieved by disrupting late-stage N-glycosylation genes (MNS1 or MNL1), overexpressing COPII vesicle assembly genes (SEC23 or SAR1), cargo receptor genes (ERV29 or EMP47) and transport factor gene (BET1), and deleting the vacuolar protease gene PRB1, while individual modifications increased LBA secretion by 16%-74%. Combining key modifications (mns1Δ, prb1Δ, and SEC23, SAR1 overexpression) with attenuation of the heme-degrading enzyme Hmx1 culminated in a secretory titer of 1.02 g/L LBA in a 5-L bioreactor, representing a 2.3-fold increase over the parental strain. The secreted LBA preserved heme-binding capacity (73.1% ratio), oxygen-binding spectral features, and peroxidase activity (956.77 U mg), confirming proper folding and functionality. Our findings establish K. marxianus as an efficient platform for producing functional, food-safe LegH, with broad implications for meat-analog development and medical applications. - Source: PubMed
Publication date: 2026/02/23
Wu XinweiFeng DidiChen HongYin AnqiTian TianZhou JungangYu YaoLu Hong - Pregnancy establishment in mammals requires a complex sequence of events, including bi-lateral embryo-maternal communication, leading up to implantation. This is the time when most pregnancy loss occurs in mammals (including humans and food production species) and dysregulation in embryo-maternal communication contributes to pregnancy loss. Embryo-derived factors modify the function of the endometrium for pregnancy success. We hypothesise that these previously unexplored conceptus-derived proteins may be involved in altering the function of the endometrium to facilitate early pregnancy events in mammals with different early pregnancy phenotypes. Here, we show that protein disulphide-isomerase (PDI) is a highly conserved protein among mammals and provide evidence for a species-specific role for PDI in endometrial function in mammals with different implantation strategies. We show how PDI alters the endometrial transcriptome in human and bovine in vitro in a species-specific manner and using a microfluidic approach we demonstrate that it alters the secretome capability of the endometrium. We also provide evidence from in vitro assays using human-derived cells that MNS1, a transcript commonly downregulated in response to PDI in human and bovine endometrial epithelial cells, may be involved in the attachment phase of implantation. We propose that the trophoblast-derived protein PDI, is involved in supporting the modulation of the uterine luminal fluid (ULF) secreted by the endometrium to support conceptus nourishment, and in the process of embryo attachment to the uterine lumen for pregnancy success in mammals. - Source: PubMed
Tinning HaideeTaylor AlyshaWang DapengPullinger AnnaOikonomou GeorgiosVelazquez Miguel AThompson PaulTreumann AchimRuane Peter TO'Connell Mary JForde Niamh - Infertility affects approximately 15% of couples globally, with male factors contributing to nearly 50% of cases. However, the genetic basis of male infertility, particularly idiopathic forms, remains poorly understood. In this study, we performed whole-genome sequencing (WGS) on eight normozoospermic men and nine men with oligozoospermia, asthenozoospermia, or both, followed by Sanger sequencing for validation. Comparative analysis revealed a higher burden of genomic variants in the sperm dysfunction infertility group (SDIG) than in the normozoospermic group (NG). Several nonsynonymous missense variants were exclusively identified in SDIG, including DNAJB13 (p.Ile159Asn), MNS1 (p.Asp217Asn), DNAH6 (p.Ser2210Leu), HYDIN (p.Gly901Ala, p.Arg568Trp), DNAH7 (p.Arg1486His, p.Gly171Arg, p.Ser2368Phe), DNAH17 (p.Ala3135Val), and CATSPER1 (p.Arg558Trp). These variants are predicted to affect protein structure, stability, or interactions, and were classified as variants of uncertain significance. Moreover, several variants were classified as likely pathogenic: a frameshift mutation in DNAH2 (p.Lys1414ArgfsTer29) likely resulting in a truncated protein, a missense mutation in CFAP61 (p.Arg568Trp) predicted to impair protein function, and two nonsense mutations in FSIP2 (p.Gln5809Ter and p.Cys8Ter) introducing premature stop codons. These alterations implicate key components of sperm flagellar function and motility. Our findings reveal novel and potentially deleterious genetic variants associated with male infertility, offering new insights into its molecular underpinnings and informing future diagnostic and therapeutic approaches. - Source: PubMed
Publication date: 2025/10/20
Khan Muhammad RiazShah Aftab AliAl Smadi Mohammad ALudwig NicoleFischer UlrikeAbdul-Khaliq HashimMeese EckartAbu-Halima Masood