SML0379
Nodinitib-1
≥98% (HPLC)
Synonyme(s) :
1-[(4-Methylphenyl)sulfonyl]-1H-benzimidazol-2-amine, CID-1088438, ML130
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A propos de cet article
Formule empirique (notation de Hill) :
C14H13N3O2S
Numéro CAS:
Poids moléculaire :
287.34
NACRES:
NA.77
PubChem Substance ID:
UNSPSC Code:
51111800
MDL number:
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Laissez-nous vous aiderInChI
1S/C14H13N3O2S/c1-10-6-8-11(9-7-10)20(18,19)17-13-5-3-2-4-12(13)16-14(17)15/h2-9H,1H3,(H2,15,16)
SMILES string
NC1=NC2=C(N1S(C3=CC=C(C)C=C3)(=O)=O)C=CC=C2
InChI key
SRFABRWQVPCPRG-UHFFFAOYSA-N
assay
≥98% (HPLC)
form
powder
color
white to beige
solubility
DMSO: >10 mg/mL
storage temp.
2-8°C
Quality Level
Catégories apparentées
Biochem/physiol Actions
Nodinitib-1 (ML130) is a selectiove inhibitor of of the nucleotide oligomerization domain (NOD)-1 receptor, which is involved in innate immune response and has been associated with several inflammatory diseases. NOD1 and NOD2 recognize distinct structures derived from bacterial peptidoglycans and directly activate NF-?B pathway, which controls the production of proinflammatory molecules. Nodinitib-1 has 40:1 selectivity for NOD1 over NOD2.
Nodinitib-1 is a selective inhibitor of of the nucleotide oligomerization domain (NOD)-1 receptor.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Journal of neuroinflammation, 17(1), 364-364 (2020-12-03)
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Epidemiologic studies have reported an inverse relationship between childhood Helicobacter pylori infection and development of allergic asthma. Because lung epithelium plays an important role in allergic asthma pathogenesis, we hypothesized that H. pylori may directly influence airway epithelial cell innate
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Yi-Hsin Fan et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(48), E7818-E7827 (2016-11-20)
Induction of nucleotide-binding oligomerization domain 2 (NOD2) and downstream receptor-interacting serine/threonine-protein kinase 2 (RIPK2) by human cytomegalovirus (HCMV) is known to up-regulate antiviral responses and suppress virus replication. We investigated the role of nucleotide-binding oligomerization domain 1 (NOD1), which also
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