SIL1, 32-461aa, Recombinant Protein
- Known as:
- SIL1, 32-461aa, Recombinant Protein
- Catalog number:
- GWB-P0458C
- Product Quantity:
- 20ug
- Category:
- -
- Supplier:
- GenWay
- Gene target:
- SIL1 32-461aa Recombinant Protein
Ask about this productRelated genes to: SIL1, 32-461aa, Recombinant Protein
- Gene:
- SIL1 NIH gene
- Name:
- SIL1 nucleotide exchange factor
- Previous symbol:
- MSS
- Synonyms:
- BAP, ULG5
- Chromosome:
- 5q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 2005-09-01
- Date modifiied:
- 2016-10-05
Related products to: SIL1, 32-461aa, Recombinant Protein
Related articles to: SIL1, 32-461aa, Recombinant Protein
- Gliomas are aggressive brain tumors associated with a poor prognosis. Although SIL1, an endoplasmic reticulum chaperone factor, is known to maintain protein homeostasis, its specific role in glioma pathogenesis remains poorly understood. This study aimed to investigate the clinical significance and biological functions of SIL1 in glioma. - Source: PubMed
Publication date: 2026/06/29
Liu PeiruPeng YaoSun YingHu ShenghuiLv DongyangYan Ying - This study investigated the chemical composition, fermentation dynamics, fatty-acid profile, and polyphenolic evolution of two mixed silages designed to valorize agro-industrial by-products for ruminant feeding. Silages were produced by co-ensiling wheat straw, cheese-whey, and molasses with grape pomace (SIL-1) or olive mill wastewater (SIL-2), and were monitored over a 150-day ensiling period. The two formulations exhibited distinct compositional characteristics and fermentation kinetics. SIL-1 showed higher crude protein content and a more favorable fatty-acid profile, with greater levels of selected long-chain fatty acids, whereas SIL-2 had higher dry matter and structural fiber fractions. Both silages achieved effective fermentation, reaching stable acidic conditions (pH < 4.0), although SIL-1 consistently maintained lower pH and higher buffering capacity. Fermentation end-products differed between silages, with higher concentrations of short-chain fatty acids in SIL-1 and greater lactic acid accumulation in SIL-2, under significant treatment × time interactions. Bioactive compound analysis revealed higher total phenolic content and antioxidant capacity in SIL-1, whereas SIL-2 showed marked degradation of phenolic compounds, including the loss of characteristic secoiridoids. Polyphenolic profiles displayed compound-specific temporal dynamics during ensiling. Overall, both silages were well preserved; however, SIL-1 demonstrated superior nutritional quality and bioactive stability, supporting its potential as a functional feed ingredient for ruminant nutrition. - Source: PubMed
Publication date: 2026/05/30
Dibenedetto Roberta SavinaSánchez-Parra MónicaOrdóñez-Díaz José LuisDi Luca AlessioMartemucci GiovanniMoreno-Rojas José ManuelD'Alessandro Angela Gabriella - - Source: PubMed
Publication date: 2026/05/29
Ram N AravindVijayaraghavan AsishKoshy Kiren GNair Sruthi SKrishnan Syam - The catalytic activity of silanol groups in zeolites has long been overlooked because of their much lower acidity compared to Brønsted acid sites. Here, we demonstrate their non-negligible catalytic role in methanol conversion using pure silica MFI zeolite (Silicalite-1). Two silicalite-1 samples with different crystal sizes, micron-sized (Sil1_micro) and nano-sized (Sil1_nano), were synthesized and investigated by in situ and operando FTIR spectroscopy using probe molecules (carbon monoxide, pyridine, and methanol). multivariate-curve regression by alternating least squares was applied to elucidate the influence of the silanol hydrogen-bonding network on catalytic reactivity. Distinct acid-base behaviors were identified: isolated and weakly hydrogen-bonded silanols are active at low temperatures, whereas strongly hydrogen-bonded silanols become catalytically relevant at higher temperatures. Methanol adsorption studies reveal a unique bidentate coordination mode in Sil1_nano, associated with weakly hydrogen-bonded geminal silanols, which promotes the formation of reactive intermediates and dual coke species. In contrast, Sil1_micro, characterized by a higher fraction of strongly hydrogen-bonded silanols, exhibits a different methanol reactivity pattern. These results demonstrate that silanol groups are active functional entities rather than passive defects, capable of driving methanol reforming-like transformations and steering coke formation pathways. - Source: PubMed
Publication date: 2026/05/26
Dalena FrancescoDib EddyAitblal AbdelhafidWu JunweiGhojavand SajjadZapelini IagoPiva Diógenes HonoratoMintova Svetlana - Marinesco-Sjögren Syndrome (MSS) is a rare genetic disorder characterized by cerebellar ataxia, congenital cataracts, and progressive myopathy. Approximately 60% of cases result from SIL1 gene mutations, causing endoplasmic reticulum stress and neuromuscular degeneration. We investigated AAV8-mediated SIL1 gene replacement combined with TAT peptide-mediated protein delivery in the woozy (Sil1) mouse model. Thirty-two female Sil1 mice received either AAV8-SIL1-TAT vector (5 × 10 genome copies) or saline intravenously at 4 weeks of age. The construct enabled liver-produced SIL1 protein uptake by peripheral tissues. Motor performance, cognitive behaviour, and molecular changes were monitored over 20 weeks. Treated mice showed significant motor improvement versus controls. Accelerating rotarod testing revealed delayed motor deficit onset by approximately 3 weeks, with significantly higher performance from weeks 10-14 (p < 0.001). Beam walking assessment showed reduced traversal time and contralateral falls from week 9 onwards. Western blotting and immunohistochemistry confirmed intracellular SIL1 localization in hepatocytes and muscle fibres, but not cerebellum. Quadriceps SIL1 delivery peaked at 2 weeks post-treatment, then gradually declined. Treatment normalized peIF2α and LC3 expression in quadriceps, indicating reduced ER stress and autophagy in skeletal muscle. This study provides proof-of-concept evidence for liver-based protein production combined with cell-penetrating peptides as a viable approach for treating peripheral manifestations of multisystemic disorders, while highlighting the need for alternative CNS delivery strategies for comprehensive therapeutic coverage in MSS. - Source: PubMed
Publication date: 2026/05/02
Bellia FabioRuggieri Anna GiuliaAmodei LauraPotenza FrancescaDufrusine BeatricePanella ValeriaDel Pizzo FrancescoLamolinara AlessiaIezzi ManuelaFederici LucaSallese Michele