SML1620
NGI-1
≥95% (HPLC)
Synonyme(s) :
5-[(Dimethylamino)sulfonyl]-N-(5-methyl-2-thiazolyl)-2-(1-pyrrolidinyl)-benzamide, ML414
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About This Item
Formule empirique (notation de Hill):
C17H22N4O3S2
Numéro CAS:
Poids moléculaire :
394.51
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77
Produits recommandés
Niveau de qualité
Pureté
≥95% (HPLC)
Forme
powder
Couleur
white to beige
Solubilité
DMSO: 5 mg/mL, clear (warmed)
Température de stockage
2-8°C
Catégories apparentées
Actions biochimiques/physiologiques
NGI-1 (ML414) is an inhibitor of Asparagine (N)-linked glycoslysation. NGI-1 inhibits the oligosaccharyltransferase, preventing the attachment to the protein. NGI-1 has been shown to induce senescence in receptor tyrosine kinase dependent tumors.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
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Danielle Skropeta
Bioorganic & medicinal chemistry, 17(7), 2645-2653 (2009-03-17)
In a series of investigations, N-glycosylation has proven to be a key determinant of enzyme secretion, activity, binding affinity and substrate specificity, enabling a protein to fine-tune its activity. In the majority of cases elimination of all putative N-glycosylation sites
Angelyn Larkin et al.
Biochemistry, 50(21), 4411-4426 (2011-04-22)
Asparagine-linked glycosylation involves the sequential assembly of an oligosaccharide onto a polyisoprenyl donor, followed by the en bloc transfer of the glycan to particular asparagine residues within acceptor proteins. These N-linked glycans play a critical role in a wide variety
Cecilia Lopez-Sambrooks et al.
Nature chemical biology, 12(12), 1023-1030 (2016-10-25)
Asparagine (N)-linked glycosylation is a protein modification critical for glycoprotein folding, stability, and cellular localization. To identify small molecules that inhibit new targets in this biosynthetic pathway, we initiated a cell-based high-throughput screen and lead-compound-optimization campaign that delivered a cell-permeable
Ryan A Flynn et al.
Cell, 184(12), 3109-3124 (2021-05-19)
Glycans modify lipids and proteins to mediate inter- and intramolecular interactions across all domains of life. RNA is not thought to be a major target of glycosylation. Here, we challenge this view with evidence that mammals use RNA as a
Shih-Han Wang et al.
American journal of cancer research, 12(10), 4721-4736 (2022-11-17)
N-linked glycosylation of proteins is one of the post-translational modifications (PTMs) that shield tumor antigens from immune attack. Signaling lymphocytic activation molecule family 7 (SLAMF7) suppresses cancer cell phagocytosis and is an ideal target under clinical development. PTM of SLAMF7
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