NuPAGE™ MES SDS Running Buffer (20X)
NuPAGE™ MES SDS Running Buffer (20X)
Citations & References (5)
Invitrogen™

NuPAGE™ MES SDS Running Buffer (20X)

NuPAGE MES SDS Running Buffer (20X) is formulated for running proteins on NuPAGE Bis-Tris gels. It is recommended for separatingRead more
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Catalog NumberQuantity
NP0002500 mL
NP0002025 L
Catalog number NP0002
Price (EUR)
113,65
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127,00
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Quantity:
500 mL
Price (EUR)
113,65
Online Exclusive
127,00
Save 13,35 (11%)
Each
Add to cart
NuPAGE MES SDS Running Buffer (20X) is formulated for running proteins on NuPAGE Bis-Tris gels. It is recommended for separating small- to medium-sized proteins.

Use the right buffer to optimize protein separations
NuPAGE MES SDS Running Buffer and NuPAGE MOPS SDS Running Buffer can both be used with NuPAGE Bis-Tris gels. MES has a lower pKa than MOPS, making the MES SDS Running Buffer faster than the MOPS SDS running buffers. The difference in ion migration affects stacking and results in a difference in protein separation range between these buffers. Use of MOPS buffer allows proteins to run slower than when using MES buffer.

Compare protein migration patterns using MES and MOPs on NuPAGE Bis-Tris gels

See all available buffers and reagents available for SDS-PAGE

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical Name or MaterialRunning Buffer
Formulation1X: 50 mM MES, 50 mM Tris Base, 0.1% SDS, 1 mM EDTA, pH 7.3
Recommended StorageContents: NuPAGE™ MES SDS Running Buffer (20X)
Storage: +4°C to 25°C
Solubility InformationWater
Concentration20X
Physical FormLiquid
Product LineNuPAGE
Quantity500 mL
pH7.3
Unit SizeEach

Frequently asked questions (FAQs)

Can I prepare my protein sample with the reducing agent and store it for future use?

DTT is not stable, so it must be added and the reduction performed just prior to loading your samples.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

My LDS or SDS sample buffer precipitates when stored at 4 degrees C. Can I warm it up? Can I store it at room temperature?

Precipitation of the LDS or SDS at 4 degrees C is normal. Bring the buffer to room temperature and mix until the LDS/SDS goes into solution. If you do not want to wait for it to dissolve, you can store the sample buffer at room temperature.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

How are Bolt gels different than NuPAGE gels?

While they are both Bis-Tris based gels, the chemistries are very different since Bolt gels are optimized for western blotting. Another key difference is the wedge well design of the Bolt gels, which allows larger sample volumes to be loaded.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

What is the advantage of NuPAGE Gels over regular Tris-Glycine gels?

The neutral operating pH of the NuPAGE Gels and buffers provides following advantages over the Laemmli system:
-Longer shelf life of 8-12 months due to improved gel stability
-Improved protein stability during electrophoresis at neutral pH resulting in sharper band resolution and accurate results (Moos et al, 1998)
-Complete reduction of disulfides under mild heating conditions (70 degrees C for 10 min) and absence of cleavage of asp-pro bonds using the NuPAGE LDS Sample buffer (pH > 7.0 at 70 degrees C)
-Reduced state of the proteins maintained during electrophoresis and blotting of the proteins by the NuPAGE Antioxidant
Please refer to the following paper: Moos M Jr, Nguyen NY, Liu TY (1988) Reproducible High Yield Sequencing of Proteins Electrophoretically Separated and Transferred to an Inert Support. J Biol Chem 263:6005-6008.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

Are the NuPAGE buffers/components (i.e., sample buffer, running buffer, and antioxidant) compatible with Bolt gels?

Yes, NuPAGE buffers/components are compatible with Bolt gels.

Find additional tips, troubleshooting help, and resources within our Protein Electrophoresis and Western Blotting Support Center.

View all NuPAGE™ MES SDS Running Buffer (20X), 500 mL FAQs

Citations & References (5)

Citations & References
Abstract
Matrix GLA protein, a regulatory protein for bone morphogenetic protein-2.
Authors: Zebboudj Amina F; Imura Minori; Boström Kristina;
Journal:J Biol Chem
PubMed ID:11741887
'Matrix GLA protein (MGP) has been identified as a calcification inhibitor in cartilage and vasculature. Part of this effect may be attributed to its influence on osteoinductive activity of bone morphogenetic protein-2 (BMP-2). To detect binding between MGP and BMP-2, we performed immunoprecipitation using MGP and BMP-2 tagged with FLAG ... More
Oligomerization of the integrin alphaIIbbeta3: roles of the transmembrane and cytoplasmic domains.
Authors: Li R; Babu C R; Lear J D; Wand A J; Bennett J S; DeGrado W F;
Journal:Proc Natl Acad Sci U S A
PubMed ID:11606749
'Integrins are a family of alpha/beta heterodimeric membrane proteins, which mediate cell-cell and cell-matrix interactions. The molecular mechanisms by which integrins are activated and cluster are currently poorly understood. One hypothesis posits that the cytoplasmic tails of the alpha and beta subunits interact strongly with one another in a 1:1 ... More
beta -Glucoside Kinase (BglK) from Klebsiella pneumoniae. PURIFICATION, PROPERTIES, AND PREPARATIVE SYNTHESIS OF 6-PHOSPHO-beta -D-GLUCOSIDES.
Authors: Thompson John; Lichtenthaler Frieder W; Peters Siegfried; Pikis Andreas;
Journal:J Biol Chem
PubMed ID:12110692
ATP-dependent beta-glucoside kinase (BglK) has been purified from cellobiose-grown cells of Klebsiella pneumoniae. In solution, the enzyme (EC ) exists as a homotetramer composed of non-covalently linked subunits of M(r) approximately 33,000. Determination of the first 28 residues from the N terminus of the protein allowed the identification and cloning ... More
An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system.
Authors: Kiga Daisuke; Sakamoto Kensaku; Kodama Koichiro; Kigawa Takanori; Matsuda Takayoshi; Yabuki Takashi; Shirouzu Mikako; Harada Yoko; Nakayama Hiroshi; Takio Koji; Hasegawa Yoshinori; Endo Yaeta; Hirao Ichiro; Yokoyama Shigeyuki;
Journal:Proc Natl Acad Sci U S A
PubMed ID:12097643
Tyrosyl-tRNA synthetase (TyrRS) from Escherichia coli was engineered to preferentially recognize 3-iodo-L-tyrosine rather than L-tyrosine for the site-specific incorporation of 3-iodo-L-tyrosine into proteins in eukaryotic translation systems. The wild-type TyrRS does not recognize 3-iodo-L-tyrosine, because of the bulky iodine substitution. On the basis of the reported crystal structure of Bacillus ... More
Adverse drug reactions.
Authors:Patton K,Borshoff DC
Journal:Anaesthesia
PubMed ID:29313907