SND1 purified MaxPab mouse polyclonal antibody (B02P)
- Known as:
- SND1 enriched MaxPab mouse pab (anti-) (B02P)
- Catalog number:
- H00027044-B02P
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SND1 purified MaxPab mouse polyclonal antibody (B02P)
Related genes to: SND1 purified MaxPab mouse polyclonal antibody (B02P)
- Gene:
- SND1 NIH gene
- Name:
- staphylococcal nuclease and tudor domain containing 1
- Previous symbol:
- -
- Synonyms:
- TDRD11, p100
- Chromosome:
- 7q32.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-12-19
- Date modifiied:
- 2016-10-05
Related products to: SND1 purified MaxPab mouse polyclonal antibody (B02P)
Related articles to: SND1 purified MaxPab mouse polyclonal antibody (B02P)
- The metadherin (MTDH)-staphylococcal nuclease domain-containing protein 1 (SND1) interaction is an oncogenic protein-protein interaction (PPI) linked to cancer cell survival, progression, and metastasis, but small-molecule disruptors remain scarce. Here, we developed an integrated in silico-to-in vitro workflow to discover 1 H-indazole-3-carboxylic acid derivatives as MTDH-SND1 PPI disruptors. A focused library of 399 compounds was processed through a funnel-based screening pipeline comprising drug-likeness and PAINS/reactivity filtering, diversity/purchasability triage, AutoDock Vina docking, and short molecular dynamics (MD) refinement with MM/PBSA rescoring. Three compounds (IC1-IC3) were prioritized for 1,000-ns MD simulations and mechanistic analysis. Docking and MD showed that all three compounds bind the targeted SND1 interfacial groove, but with different functional consequences. PPI-oriented MM/PBSA, FEL, and trajectory-based disruption metrics consistently ranked IC2 as the strongest predicted disruptor, IC1 as a moderate disruptor, and IC3 as a non-disruptive interfacial binder despite favorable direct binding energy. Free-energy landscape analysis further showed that IC2 most strongly remodeled the conformational landscape of the MTDH-SND1 complex, whereas IC3 remained confined to a more stable, non-disruptive basin. Split-luciferase complementation assays validated these predictions. In cell-free assays, IC values were 2.94 ± 0.35 µM (IC2), 4.19 ± 0.48 µM (IC1), and 116.29 ± 5.21 µM (IC3). In SCP28 cell-based assays, IC values were 12.08 ± 1.4 µM, 18.0 ± 2.1 µM, and 337 ± 12.9 µM, respectively, while linked-luciferase counter-screen IC values exceeded 1,000 µM for all compounds. ADMETlab 3.0 profiling identified IC1 as the most balanced developability candidate, whereas IC2 remained the lead efficacy-prioritized hit for subsequent optimization efforts. - Source: PubMed
Publication date: 2026/05/28
Kamel Emadeldin MKhadrawy Sally MostafaAllam Ahmed AOthman Sarah IAbalkhail AdilAlkhayl Faris F AbaLamsabhi Al Mokhtar - Alterations of BRAF, most commonly the V600E point mutation, are uncommon in salivary gland tumors, while BRAF fusions are exceptionally rare. We report four salivary gland tumors harboring BRAF fusions. The cohort included three males and one female aged 30-67 years (median, 46 years), all with tumors arising in the parotid gland. Two tumors were classified as intraductal carcinoma of oncocytic and mixed oncocytic-intercalated duct subtype, harboring AGK::BRAF and PAPSS1::BRAF fusions. In both cases, tumor cells were positive for S100, SOX10, and mammaglobin, and negative for androgen receptor. One tumor was diagnosed as low-grade acinic cell carcinoma with an SND1::BRAF fusion; tumor cells expressed SOX10, DOG1, and NR4A2 (Nurr1), but were negative for S100 and NOR1. The fourth tumor, classified as high-grade salivary adenocarcinoma, not otherwise specified, harbored an AGK::BRAF fusion and showed unusual morphology, including monolayered tubules and trabeculae, and focal papillary formations. Tumor cells were columnar with enlarged, overlapping vesicular nuclei and pale cytoplasm, expressing GATA3, S100, SOX10, and DOG1, while lacking mammaglobin expression. Focal p63/p40 positivity suggested a possible preexisting in situ component. BRAF fusions are exceedingly rare in salivary gland tumors and may occur across different histologic types. Given their potential sensitivity to MEK or next-generation RAF inhibitors, comprehensive molecular testing is essential for identifying patients who may benefit from targeted therapies. - Source: PubMed
Publication date: 2026/05/22
Laco JanBradová MartinaMauramo MattiVaněček TomášKohout AlešHájek JosefHácová MáriaLeivo IlmoMolony PeterJirásek TomášAgaimy AbbasSkálová Alena - Staphylococcal nuclease and Tudor domain‑containing protein 1 (SND1) is a multifunctional RNA‑binding protein implicated in transcriptional regulation, post‑transcriptional RNA control, oncogenesis, and viral infection. Initially identified as a transcriptional coactivator, SND1 was later established as a component of the RNA‑induced silencing complex, where it contributes to RNA turnover and microRNA regulation. SND1's diverse activities stem from its modular architecture, comprising four staphylococcal nuclease‑like domains, capable of direct RNA binding, and an extended Tudor domain that together form an integrated RNA‑binding and catalytic platform. This versatility also underlies its role in viral infection: SND1 acts as an m⁶A reader and is exploited by RNA viruses, such as SARS‑CoV‑2. Recent work showed that SND1 depletion, particularly loss of its third structured domain (SN3), reduces recruitment of the viral protein Nsp9 to the 3' untranslated region of the SARS‑CoV‑2 genome, impairing viral RNA synthesis through a direct SN3-Nsp9 interaction. Here, we report expression, purification, and near‑complete backbone NMR assignments of the SN3 domain of SND1. Secondary structure elements calculated by TALOS-N based on these assignments are in good agreement with the existing crystal structure of SN3. Our data provide an excellent foundation for future structural studies of SND1-RNA complexes and their roles in viral RNA priming in SARS-CoV-2. - Source: PubMed
Publication date: 2026/05/16
Ajith ShradhaCubeddu LizaGamsjaeger Roland - - Source: PubMed
Publication date: 2026/04/16
Li YingYang ChengruCui GuoliGui ShiliangJia LinlinChen YuNiu HonglinXin Hua - - Source: PubMed
Publication date: 2026/04/10
Zhan FuliangZhong YanyingQin YunnaLi LiangWu WenwenYao Meizhen