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80827

Supelco

N,N-Dimethyl-2-sulfamoylnicotinamide

PESTANAL®, analytical standard

Synonym(s):

2-(Aminosulfonyl)-N,N-dimethyl-3-pyridinecarboxamide, 2-Aminosulfonyl-N,N-dimethylnicotinamide, N,N-Dimethyl-2-sulfamoylpyridine-3-carboxamide

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About This Item

Empirical Formula (Hill Notation):
C8H11N3O3S
CAS Number:
112006-75-4
Molecular Weight:
229.26
Beilstein:
9193761
MDL number:
MFCD03265507
UNSPSC Code:
12352200
PubChem Substance ID:
329769061

grade

analytical standard

product line

PESTANAL®

Assay

≥98.0% (HPLC)

shelf life

limited shelf life, expiry date on the label

format

neat

storage temp.

2-8°C

SMILES string

O=C(N(C)C)C1=CC=CN=C1S(=O)(N)=O

InChI

1S/C8H11N3O3S/c1-11(2)8(12)6-4-3-5-10-7(6)15(9,13)14/h3-5H,1-2H3,(H2,9,13,14)

InChI key

WYFKZPLSYVJLRB-UHFFFAOYSA-N

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Legal Information

PESTANAL is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H317,H412

Hazard Classifications

Aquatic Chronic 3 - Skin Sens. 1

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
BCCB0309
BCBR9508V
BCBR9508
BCBR1562

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Mette C Jørgensen et al.
Development (Cambridge, England), 145(17) (2018-08-11)
Mutations in Hes1, a target gene of the Notch signalling pathway, lead to ectopic pancreas by a poorly described mechanism. Here, we use genetic inactivation of Hes1 combined with lineage tracing and live imaging to reveal an endodermal requirement for
Vladislav Belyy et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(3), 1533-1542 (2019-12-25)
The endoplasmic reticulum (ER) membrane-resident stress sensor inositol-requiring enzyme 1 (IRE1) governs the most evolutionarily conserved branch of the unfolded protein response. Upon sensing an accumulation of unfolded proteins in the ER lumen, IRE1 activates its cytoplasmic kinase and ribonuclease
Diogo R Feleciano et al.
Frontiers in aging neuroscience, 11, 9-9 (2019-02-15)
A functional protein quality control machinery is crucial to maintain cellular and organismal physiology. Perturbation in the protein homeostasis network can lead to the formation of misfolded and aggregated proteins that are a hallmark of protein conformational disorders and aging.
María Expósito-Serrano et al.
Current biology : CB, 30(16), 3212-3222 (2020-06-06)
An important question in cell biology is how cellular organelles partition during cell division. In organisms undergoing closed mitosis, the elongation of an intranuclear spindle drives nuclear division, generating two identically sized nuclei [1, 2]. However, how the site of
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