MOPS 1 kg

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Price:

$41.00

SKU:

CI-00217-100G

MOPS

(3-(N-morpholino)propanesulfonic acid; 4-Morpholinepropanesulfonic acid)

Purity > 99.5 %

CAS Number:	1132-61-2
Chemical Formula:	C₇H₁₅NO₄S
Molecular Weight:	209.3 g/mol

MOPS buffer is used for the electrophoresis of RNA through agarose gels. In cell biology, MOPS can be used for the isolation of plant organelles such as chloroplasts. Useful pH Range6.5 - 7.9

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Protocol for the Preparation of 10x MOPS Electrophoresis Buffer

1) Dissolve 41.8 g of MOPS in 700 ml of sterile DPEC treated H₂O. Adjust the pH to 7.0 N NaOH.

2) Add 20 ml of DEPC treated 1 M sodium acetate and 20 ml of DEPC treated of 0.5 M EDTA pH 8.0. Adjust the volume of the solution to 1 L with DEPC treated H₂O.

3) Sterilize by filtering through a 0.45 um and store protected from sunlight.

The purpose of DEPC (diethylpyrocarbonate) is to eliminate RNAse activity.

Required Reagents

20 mM sodium acetate trihydrate

10 mM EDTA pH 8.0

0.2 M MOPS pH 7.0
20 mM sodium acetate trihydrate
10 mM EDTA pH 8.0

Celebrity Endorsements

Kandegedara, A., Rorabacher, D.B. (1999) Noncomplexing Tertiary Amines as “Better” Buffers Covering the Range of pH 3− 11. Temperature Dependence of Their Acid Dissociation Constants. Anal. Chem., 71 (15), 3140–3144.
-The paper examines a number of buffers developed by Good (often called “Good’s” or “Good” buffers) have been shown to cause metal ion interference as a result of complexation. This can be critical in protein crystallization especially if metals are needed for proper protein folding. A series of tertiary amines, devoid of hydroxy groups or other weak donors on the r, â, or ç carbons, have been developed as “Better” pH buffers which, as a result of steric hindrance, are incapable of forming even weak complexes with metal ions. MOPS, MES and PIPES are the only three of the twenty Good Buffers that were examined that do not show weak coordination. Unfortunately, PIPES can be limited due to solubility in biologically relevant conditions.

Goldber, DA. (1980) Isolation and partial characterization of the Drosophila alcohol dehydrogenase gene. Proc. Natl. Acad. Sci. USA. Vol. 77, 5794-5798.

Oldfield, TJ. Ceska, TA. Brady, RL. (1991) A flexible approach to automated protein crystallization. Journal of Applied Crystallography. Vol. 24. 255-260.
-MOPS is used as an example buffer in this paper discussing a set up for automated protein crystallization.