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C9630

Cytidine 2′:3′-cyclic monophosphate monosodium salt

≥95% (HPLC), synthetic, powder

Synonym(s):

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

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100 MG

CHF 346.00

250 MG

CHF 604.00

CHF 346.00

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About This Item

Empirical Formula (Hill Notation):
C9H11N3NaO7P
CAS Number:
15718-51-1
Molecular Weight:
327.16
Beilstein:
4086446
EC Number:
239-813-2
MDL number:
MFCD00135656
UNSPSC Code:
41106305
PubChem Substance ID:
24893179
NACRES:
NA.51

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Product Name

Cytidine 2′:3′-cyclic monophosphate monosodium salt, ≥95% (HPLC)

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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This Item
A9376G6129SML1229
Cytidine 2′:3′-cyclic monophosphate monosodium salt ≥95% (HPLC)

Sigma-Aldrich

C9630

Cytidine 2′:3′-cyclic monophosphate monosodium salt

Adenosine 2′:3′-cyclic monophosphate sodium salt ≥93%

Sigma-Aldrich

A9376

Adenosine 2′:3′-cyclic monophosphate sodium salt

Guanosine 3′,5′-cyclic monophosphate sodium salt ≥99% (HPLC), powder

Sigma-Aldrich

G6129

Guanosine 3′,5′-cyclic monophosphate sodium salt

2′,3′-cGAMP sodium salt ≥98% (HPLC)

Sigma-Aldrich

SML1229

2′,3′-cGAMP sodium salt

biological source

synthetic

biological source

synthetic (organic)

biological source

-

biological source

-

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

100

assay

≥95% (HPLC)

assay

≥93%

assay

≥99% (HPLC)

assay

≥98% (HPLC)

form

powder

form

powder

form

powder

form

powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

solubility

water: 50 mg/mL, clear, colorless

solubility

water: 50 mg/mL, clear, colorless

solubility

H2O: 50 mg/mL

solubility

-

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
BCCM8993
BCCL6935
BCCK3105
BCCL1251
BCCH1540

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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
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
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.
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
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
View All Related Papers

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