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C9630

Sigma-Aldrich

Cytidine 2′:3′-cyclic monophosphate monosodium salt

≥95% (HPLC)

Sinónimos:

2′,3′-cCMP, 2′,3′-Cyclic CMP monosodium salt, Cyclic cytidylic acid, Cytidine 2′,3′-cyclophosphate sodium salt

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About This Item

Fórmula empírica (notación de Hill):
C9H11N3NaO7P
Número de CAS:
15718-51-1
Peso molecular:
327.16
Beilstein/REAXYS Number:
4086446
EC Number:
239-813-2
MDL number:
MFCD00135656
UNSPSC Code:
41106305
PubChem Substance ID:
24893179
NACRES:
NA.51

biological source

synthetic

assay

≥95% (HPLC)

form

powder

solubility

water: 50 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

[Na+].NC1=NC(=O)N(C=C1)[C@@H]2O[C@H](CO)[C@H]3OP([O-])(=O)O[C@@H]23

InChI

1S/C9H12N3O7P.Na/c10-5-1-2-12(9(14)11-5)8-7-6(4(3-13)17-8)18-20(15,16)19-7;/h1-2,4,6-8,13H,3H2,(H,15,16)(H2,10,11,14);/q;+1/p-1/t4-,6-,7-,8-;/m1./s1

InChI key

SQOIXCJUYWSZDW-IAIGYFSYSA-M

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Application

Cytidine 2′,3′-cyclic monophosphate (2′,3′-CyclicCMP) (2′,3′-cCMP) is used as a model substrate for kinetic analysis of various ribonucleases, especially ribonuclease A.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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pH-Stat titration allows the continuous determination of ribonuclease A activity toward cytidine 2',3'-cyclic monophosphate at high substrate concentrations.
Jens Köditz et al.
Analytical biochemistry, 305(2), 281-284 (2002-06-11)
S Adinolfi et al.
FEBS letters, 398(2-3), 326-332 (1996-12-02)
In the ribonuclease superfamily, dimericity is a unique feature of bovine seminal RNase (BS-RNase). In about two-thirds of native BS-RNase molecules, the two subunits interchange their N-terminal tails, thus generating domain-swapped dimers (MxM), which mostly responsible for enzyme biological activities
M Moussaoui et al.
The Journal of biological chemistry, 273(40), 25565-25572 (1998-09-25)
The kinetics of the hydrolysis of cytidine 2',3'-cyclic phosphate (C>p) to 3'-CMP by ribonuclease A are multiphasic at high substrate concentrations. We have investigated these kinetics by determining 3'-CMP formation both spectrophotometrically and by a highly specific and quantitative chemical
Mojca Bencina et al.
Journal of chromatography. A, 1144(1), 135-142 (2007-01-20)
In gene therapy and DNA vaccination, RNA removal from DNA preparations is vital and is typically achieved by the addition of ribonuclease into the sample. Removal of ribonuclease from DNA samples requires an additional purification step. An alternative is the
Y Markert et al.
Protein engineering, 14(10), 791-796 (2001-12-12)
Although highly stable toward unfolding, native ribonuclease A is known to be cleaved by unspecific proteases in the flexible loop region near Ala20. With the aim to create a protease-resistant ribonuclease A, Ala20 was substituted for Pro by site-directed mutagenesis.
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