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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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Shawn D Spencer et al.
Pharmaceutical research, 21(9), 1642-1647 (2004-10-23)
Isothermal titration calorimetry (ITC) and progress curve analysis was used to measure the enzyme kinetic parameters (KM and kcat) of the hydrolysis of cCMP by RNase-A, a reaction that includes end-product competitive inhibition by 3'-CMP. The heat generated from injection
M Ribó et al.
Protein expression and purification, 7(3), 253-261 (1996-05-01)
Human pancreatic ribonuclease (HP-RNase) has considerable promise as a therapeutic agent. Structure-function analyses of HP-RNase have been impeded by the difficulty of obtaining the enzyme from its host. Here, a gene encoding HP-RNase was designed, synthesized, and inserted into two
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.
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
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
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