NuPAGE™ MES SDS Running Buffer (20X)

Citations & References (5)

Invitrogen™

NuPAGE™ MES SDS Running Buffer (20X)

Name: NuPAGE™ MES SDS Running Buffer (20X)
SKU: NP0002
Price: 17500 JPY

NuPAGE MES SDS泳動バッファー（20X）は、NuPAGE Novex Bis-Trisゲルでのタンパク質泳動用に調製されています。小～中サイズのタンパク質の分離に推奨されます。タンパク質の分離を最適化する適切なバッファーをご使用ください詳細を見る

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製品番号（カタログ番号）	数量
NP0002	500 mL
NP000202	5 L

2 オプション

製品番号（カタログ番号） NP0002

価格（JPY）

17,500

Each

カートに追加

数量:

500 mL

価格（JPY）

17,500

Each

カートに追加

NuPAGE MES SDS泳動バッファー（20X）は、NuPAGE Novex Bis-Trisゲルでのタンパク質泳動用に調製されています。小～中サイズのタンパク質の分離に推奨されます。

タンパク質の分離を最適化する適切なバッファーをご使用ください
NuPAGE MES SDS泳動バッファーおよびNuPAGE MOPS SDS泳動バッファーはどちらもNuPAGE Bis-Trisゲルで使用できます。MESのpKaはMOPSよりも低いため、MES SDS泳動バッファーはMOPS SDS泳動バッファーよりも高速です。イオン移動の差異はスタッキングに影響することから、これらのバッファーでのタンパク質の分離範囲に差が生じます。MOPSバッファーを使用すると、MESバッファーを使用する場合よりもタンパク質の泳動速度を遅くすることができます。

MESを使用した場合とMOPSを使用した場合のNuPAGE Bis-Trisゲルでのタンパク質移動の比較

SDS-PAGEに使用可能なすべてのバッファーと試薬の一覧

研究用にのみ使用できます。診断用には使用いただけません。

仕様

化学物質名または材質Running Buffer

組成1X: 50 mM MES, 50 mM Tris Base, 0.1% SDS, 1 mM EDTA, pH 7.3

推奨保存方法Contents: NuPAGE™ MES SDS Running Buffer (20X)
Storage: +4°C to 25°C

溶解度情報Water

濃度20X

物理的フォームLiquid

製品ラインNuPAGE

数量500 mL

pH7.3

Unit SizeEach

よくあるご質問（FAQ）

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

引用および参考文献 (5)

引用および参考文献

Abstract

Matrix GLA protein, a regulatory protein for bone morphogenetic protein-2.

Authors: Zebboudj Amina F; Imura Minori; BostrÃ¶m 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