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Merck

B4666

Sigma-Aldrich

5-Bromo-4-chloro-3-indolyl α-D-N-acetylneuraminic acid sodium salt

≥90%, powder

Sinónimos:

X-NeuNAc

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About This Item

Fórmula lineal:
C19H21BrClN2O9Na
Número de CAS:
Peso molecular:
559.72
MDL number:
UNSPSC Code:
12352204
PubChem Substance ID:
NACRES:
NA.32

product name

5-Bromo-4-chloro-3-indolyl α-D-N-acetylneuraminic acid sodium salt, ≥90%

assay

≥90%

form

powder

solubility

water: 50 mg/mL, clear, colorless to faintly yellow

storage temp.

−20°C

SMILES string

[Na].CC(=O)NC1C(O)CC(OC1C(O)C(O)CO)(Oc2c[nH]c3ccc(Br)c(Cl)c23)C(O)=O

InChI

1S/C19H22BrClN2O9.Na.H/c1-7(25)23-15-10(26)4-19(18(29)30,32-17(15)16(28)11(27)6-24)31-12-5-22-9-3-2-8(20)14(21)13(9)12;;/h2-3,5,10-11,15-17,22,24,26-28H,4,6H2,1H3,(H,23,25)(H,29,30);;

InChI key

QOSVDASAURDXES-UHFFFAOYSA-N

Application

5-Bromo-4-chloro-3-indolyl α-D-N-acetylneuraminic acid sodium salt has been used as a substrate for determining the neuraminidase enzymatic activity of
  • avian mycoplasma samples
  • Ornithobacterium rhinotracheale, a poultry pathogen
  • canine mycoplasma samples

Substrates

Chromogenic substrate for neuraminidase

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Nga T Lao et al.
PloS one, 4(10), e7354-e7354 (2009-10-10)
Translation is most often terminated when a ribosome encounters the first in-frame stop codon (UAA, UAG or UGA) in an mRNA. However, many viruses (and some cellular mRNAs) contain "stop" codons that cause a proportion of ribosomes to terminate and
A survey of avian Mycoplasma species for neuraminidase enzymatic activity
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Veterinary Microbiology, 130(3-4), 391-397 (2008)
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Bercic RL, et al.
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Kastelic S, et al.
Veterinary Microbiology, 162(2-4), 707-712 (2013)
I Fujii et al.
Bioorganic & medicinal chemistry, 1(2), 147-149 (1993-08-01)
A chromogenic substrate 1, 5-bromo-4-chloroindol-3-yl 5-acetamido-3,5-dideoxy-alpha-D-glycero-D-galacto-2-nonulopyranosidon ic acid (X-Neu5Ac), has been synthesized to facilitate the screening of bacterial colonies or plaques for the detection of either natural or mutant neuraminidase activity. Substrate 1 was hydrolyzed by neuraminidase isolated from Clostridium

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