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Merck

95440

Sigma-Aldrich

2-乙基-5-苯基异噁唑-3'-磺酸盐

purum, ≥97.0% (T)

别名:

伍德沃德试剂 K

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About This Item

经验公式(希尔记法):
C11H11NO4S
CAS号:
分子量:
253.27
Beilstein:
4149224
EC 号:
MDL编号:
UNSPSC代码:
12352005
PubChem化学物质编号:

等级

purum

方案

≥97.0% (T)

mp

216-219 °C (dec.)

SMILES字符串

CC[n+]1ccc(o1)-c2cccc(c2)S([O-])(=O)=O

InChI

1S/C11H11NO4S/c1-2-12-7-6-11(16-12)9-4-3-5-10(8-9)17(13,14)15/h3-8H,2H2,1H3

InChI key

MWOOKDULMBMMPN-UHFFFAOYSA-N

其他说明

用于酶中羧基的改性;用于多肽合成的偶联剂

替代产品

产品编号
说明
价格

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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A A Komissarov et al.
The Journal of biological chemistry, 270(17), 10050-10055 (1995-04-28)
Woodward's reagent K (WRK) completely inactivated Escherichia coli uridine phosphorylase by reversible binding in the active site (Ki = 0.07 mM) with subsequent modification of a carboxyl (k2 = 1.2 min-1). Neither substrate alone protected uridine phosphorylase from inactivation. The
V.L. Boyd et al.
Tetrahedron Letters, 31, 3849-3849 (1990)
M S Saini et al.
Biochimica et biophysica acta, 568(2), 370-376 (1979-06-06)
Treatment of homogenous human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) with low concentrations of Woodward's reagent K (N-ethyl-5-phenylisoxazolium-3'-sulfonate) leads to a rapid loss of enzymic activity. The rate of inactivation of the enzyme is reduced in the
Hassan Faridnouri et al.
Bioelectrochemistry (Amsterdam, Netherlands), 82(1), 1-9 (2011-07-01)
This work describes the reaction mechanism for chemical modification of tyrosinase by Woodward's Reagent K and its covalent attachment to a glassy carbon electrode. The spectrophotometric studies revealed that the modification does not cause a significant structural change to tyrosinase.
Jongchan Woo et al.
Protein science : a publication of the Protein Society, 17(4), 725-735 (2008-03-25)
Renilla luciferase (RLUC) is a versatile tool for gene expression assays and in vivo biosensor applications, but its catalytic mechanism remains to be elucidated. RLUC is evolutionarily related to the alpha/beta hydrolase family. Its closest known homologs are bacterial dehalogenases

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