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Merck
CN

C101400

Sigma-Aldrich

1,2-环己二酮

97%

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别名:
1,2-Dioxocyclohexane, Cyclohexan-1,2-dione
线性分子式:
C6H8(=O)2
CAS号:
分子量:
112.13
Beilstein:
507419
EC 号:
MDL编号:
UNSPSC代码:
12352100
PubChem化学物质编号:
NACRES:
NA.22

质量水平

检测方案

97%

形式

solid

bp

193-195 °C (lit.)

mp

34-38 °C (lit.)

储存温度

2-8°C

SMILES字符串

O=C1CCCCC1=O

InChI

1S/C6H8O2/c7-5-3-1-2-4-6(5)8/h1-4H2

InChI key

OILAIQUEIWYQPH-UHFFFAOYSA-N

基因信息

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应用

精氨酸残基的特异性试剂。

WGK

WGK 3

闪点(°F)

No data available

闪点(°C)

No data available

个人防护装备

Eyeshields, Gloves, type N95 (US)


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Andres De la Rossa et al.
Nature neuroscience, 16(2), 193-200 (2013-01-08)
The molecular mechanisms that control how progenitors generate distinct subtypes of neurons, and how undifferentiated neurons acquire their specific identity during corticogenesis, are increasingly understood. However, whether postmitotic neurons can change their identity at late stages of differentiation remains unknown.
D Scott Wilbur et al.
Bioconjugate chemistry, 13(3), 611-620 (2002-05-16)
Recombinant streptavidin (rSAv) is of interest as a carrier of alpha-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting.
S Adak et al.
The Biochemical journal, 314 ( Pt 3), 985-991 (1996-03-15)
The plausible role of arginine and tyrosine residues at the active side of horseradish peroxidase (HRP) in aromatic donor (guaiacol) oxidation was probed by chemical modification followed by characterization of the modified enzyme. The arginine-specific reagents phenylglyoxal (PGO), 2,3-butanedione and
Bellamkonda Ramakrishna et al.
International journal of biological macromolecules, 115, 1225-1232 (2018-05-05)
The recombinant C-terminal domain of chitinase C of Chitinophaga pinensis (CpChiC-GH18C) exhibits the highest activity at pH 6.0 and 35 °C, with a Km of 76.13 (mg-1 ml), a kcat of 10.16 (s-1), and a kcat/Km of 0.133 (mg-1 ml s-1) on colloidal chitin. Analysis
I Heiland et al.
Biochemistry, 18(21), 4605-4612 (1979-10-16)
The primary structure of protein L21 from the 50S subunit of Escherichia coli ribosomes has been completely determined by sequencing the peptides obtained by digestion of L21 with trypsin before and after modification of the arginine residues with 1,2-cyclohexanedione, Staphylococcus

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