SP110 Mouse Polyclonal Antibody
- Known as:
- SP110 Mouse Polyclonal Antibody
- Catalog number:
- BIN-003431-B01
- Product Quantity:
- 0.05ml
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- SP110 Mouse Polyclonal Antibody
Related genes to: SP110 Mouse Polyclonal Antibody
- Gene:
- SP110 NIH gene
- Name:
- SP110 nuclear body protein
- Previous symbol:
- IFI41, IFI75
- Synonyms:
- -
- Chromosome:
- 2q37.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-12-19
- Date modifiied:
- 2019-04-23
Related products to: SP110 Mouse Polyclonal Antibody
Related articles to: SP110 Mouse Polyclonal Antibody
- Toxin-antidote (TA) systems are selfish genetic elements that bias their own inheritance by coupling a toxin that kills offspring with an antidote that specifically rescues carriers. Although widespread across bacteria, archaea, fungi, plants, and invertebrates, TA systems have not been described in vertebrates. Here we report the first vertebrate TA system, which sabotages mammalian embryogenesis. We define HEX (Homogenously staining region-mediated Embryo eXecution) as a selfish element that biases its transmission through the female mouse germline. Crosses between HEX heterozygous females and wild-type males result in selective lethality of wild-type embryos, yielding preferential survival of HEX-bearing progeny. Using mouse genetics, embryo transfer, and zygote micromanipulation, we show that HEX operates through a canonical TA mechanism: the maternally deposited toxin SP100 induces genotoxic stress in embryos, while the linked antidote SP110 selectively rescues HEX-positive embryos. Both components are core factors of the interferon signaling pathway, revealing that HEX co-opts innate immune machinery to drive transmission bias. These findings establish a vertebrate TA system and demonstrate that selfish elements can repurpose fundamental cellular pathways to violate Mendelian inheritance, with profound consequences for female fertility. - Source: PubMed
Publication date: 2026/03/25
Silva Duilio M Z ASkinner MorganTotsuka TakayaAkera Takashi - The optimal surface treatment for developing a durable bond of dual-cure self-adhesive resin cement and 3D printed hybrid ceramic has not yet been established. To evaluate the effect of Non-Thermal Atmospheric Plasma (NTAP), sandblasting (SB), and a combination of both techniques on Micro-Shear Bond Strength (µSBS) of dual-cure self-adhesive resin cement bonded to 3D printed hybrid ceramic after thermocycling, and assess the failure mode using SEM. A total of 75 resin tags of dual-cure self-adhesive resin cement (TheraCem) were cemented to fifteen discs of 3D Printed Hybrid Ceramic (Saremc- Print Crowntec) (five resin tags/ disc). Specimens were allocated into five groups according to discs’ surface treatment (n = 15); PL group: specimens were treated with NTAP, S50 group: specimens were treated with 50 μm AL2O3 SB, S110 group: treated with 110 μm AL2O3 SB, SP50 group: treated with 50 μm AL2O3 SB followed by NTAP, and SP110 group: treated with 110 μm AL2O3 SB followed by NTAP. Resin cylinders, 0.8 mm in diameter and 1 mm height, were cemented to discs. The µSBS test was performed using a universal testing machine after thermocycling. SEM was used to analyze the failure mode. Data were analyzed using Welch one-way ANOVA followed by the Games-Howell post hc test. A significant difference between groups (P = 0.026). The highest value was measured in SP50 (2.70 ± 0.49) (MPa), followed by SP110 (2.37±0.38) (MPa), then PL (2.35 ± 0.57) (MPa), and S110 (2.18 ± 0.31) (MPa), while the lowest value was found in S50 (2.12 ± 0.75) (MPa). Post hoc pairwise comparisons showed SP50 to have significantly higher values than S110 and S50 (P < 0.05). NTAP, particularly when combined with 50 μm sandblasting, improved µSBS to 3D-printed hybrid ceramics under the conditions of this in-vitro study. Clinical validation is recommended. - Source: PubMed
Publication date: 2026/04/02
El-Shazly MostafaAlkaranfilly GhadaEl-Ghazawy Mahmoud OsamaEmad BassemMahrous Aliaa - Stimulation of the innate immune system by foreign RNA elicits a potent interferon response and can trigger cell death. The mechanisms by which cells balance a robust response with cell-intrinsic lethality are still being uncovered. Here, using genome-wide CRISPR-Cas9 genetic screens with triphosphorylated RNA stimulation, we discover that promyelocytic leukaemia (PML) nuclear body-localized speckled protein 110 (SP110) is a potent inhibitor of type 1 interferon-driven cell death. Death suppression by SP110 counteracts a toxic activity of SP100, a major constituent of PML bodies. Loss of SP110 leads to mitotic retention of SP100 and PML bodies, which associate with and perturb segregating chromosomes, leading to micronucleus formation, DNA damage and genotoxic cell death. A combination of cryo-electron microscopy, AlphaFold modelling and cellular biochemistry reveals that SP110 dissolves toxic SP100 oligomers via necessary and sufficient direct interactions between their caspase activation and recruitment domains. These data reveal the critical roles of SP100 and SP110 in governing the disassembly of PML bodies during mitosis, as well as the repercussions if this process is misregulated. - Source: PubMed
Publication date: 2026/03/13
Aird Eric JRabl JuliusKnuesel TabeaGroen KevinAwwad Samah WKorablev BorisScherpe LynnAl-Herz WaleedHupfer RobinRecher MikeJackson Stephen PHale Benjamin GCorn Jacob E - Bovine tuberculosis (bTB) is a chronic debilitating zoonotic disease caused by Mycobacterium bovis (M. bovis). M. bovis exhibits a broad host range, but dairy cattle are particularly susceptible. The SP110 (speckled protein 110) gene has been demonstrated to be associated with host susceptibility to TB, but whether the susceptibility of dairy cattle to M. bovis is correlated with the bovine SP110 (bSP110) gene has not been investigated. Here, we demonstrated that the heightened susceptibility of dairy cattle to bTB was driven by species-specific alternative splicing of the bovine SP110 (bSP110) gene, which resulted in predominant expression of a truncated bSP110c variant lacking the SAND domain required for anti-bTB function. Compared to the other two splice variants of bSP110 gene, bSP110a and bSP110b, bSP110c showing significantly reduced resistance to M. bovis. Mechanistically, the ruminant-specific absence of a upstream of the SAND exon (designated as the pre-SAND exon) affects alternative splicing of the bSP110 gene, consequently promoting bSP110c production, while substituting this region with human/equine sequences introduces suppress bSP110c and increase bSP110a/b expression. Our study provides a new perspective on the genetic basis of the susceptibility of dairy cows to bTB and identifies a potential gene editing region for the breeding of tuberculosis-resistant dairy cows. - Source: PubMed
Publication date: 2025/12/12
Fan AjiaoGuo YingLi ZhunanDong XiangchenZhang ZihanWang XinyuSong YanliangHan JingYang JingWang HaoxinZhang XinyanZhang YongGao Yuanpeng - Cancer remains a leading global health burden, with projections estimating 35 million new cases by 2050. The Speckled Protein 100 (SP100) family, comprising SP100, SP110, SP140, and SP140L, has emerged as a critical player in cancer biology due to their roles in transcriptional regulation, chromatin modification, and immune signaling. While SP100 acts as a tumor suppressor in malignancies like breast cancer, SP110 and SP140 are implicated in promoting oral squamous cell carcinoma and glioma progression, respectively, and SP140L is linked to poor prognosis in pancreatic adenocarcinoma. Despite growing evidence of their dual oncogenic and tumor-suppressive functions across cancers, inconsistencies in expression patterns, regulatory mechanisms, and clinical implications persist. The current review of the SP100 family’s roles in cancer aims to clarify any direct future translational research to enhance cancer outcomes. - Source: PubMed
Publication date: 2025/11/04
Azami MehrnooshSadeghi FatemehMohammadi NazaninShayegh Zahra SadatHassanzadeh ArshiaHeidarzadeh Mohammad JavadZarinKhat ArminMohamadi Zhina