NuPAGE™ Bis-Tris Mini Protein Gels, 12%, 1.0 mm
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NuPAGE™ Bis-Tris Mini Protein Gels, 12%, 1.0 mm
NuPAGE™ Bis-Tris Mini Protein Gels, 12%, 1.0 mm
NuPAGE™ Bis-Tris Mini Protein Gels, 12%, 1.0 mm
Invitrogen™

NuPAGE™ Bis-Tris Mini Protein Gels, 12%, 1.0 mm

NuPAGE™ Novex™ 12% Bis-Trisゲルは、変性条件下で小∼中サイズのタンパク質を最適に分離するように設計されたプレキャストポリアクリルアミドゲルです。
製品番号(カタログ番号)ウェル数量
NP0341BOX10ウェル10ゲル/箱
NP0341PK210ウェル2ゲル/箱
NP0342BOX12ウェル10ゲル/箱
NP0342PK212ウェル2ゲル/箱
NP0343BOX15ウェル10ゲル/箱
NP0344BOX1ウェル10ゲル/箱
NP0346BOX2Dウェル10ゲル/箱
NP0349BOX17ウェル10ゲル/箱
製品番号(カタログ番号) NP0341BOX
価格(JPY)
27,500
Each
お問い合わせください ›
ウェル:
10ウェル
数量:
10ゲル/箱

NuPAGE™ Novex™ 12% Bis-Trisゲルは、変性条件下で小∼中サイズのタンパク質を最適に分離するように設計されたプレキャストポリアクリルアミドゲルです。従来のトリス-グリシンゲルとは異なり、NuPAGE™ Novex™ ビス-トリスゲルは中性のpH環境で、タンパク質の修飾を最小限に抑えます。NuPAGE™ Novex™ Bis-Trisゲルは、シーケンシング、質量分析、およびタンパク質の完全性が重要なその他の技法でタンパク質を調製する場合に使用します。

NuPAGE Bis-Trisゲルの特長:
より優れたタンパク質の統合性—最適化されたサンプル調製プロセスタンパク質により、タンパク質が保護されます
分子量の幅広い分離—適切なゲルと泳動バッファーを選択して、タンパク質を最適に分離します。
迅速な泳動—タンパク質の分離をわずか 35分で行えます。
長い製品寿命—NuPAGE ビス-トリスゲルは室温で 12ヵ月以上保存できます。

タンパク質分離に適した NuPAGE ビス-トリスゲルを選択してください。
ゲルと泳動バッファーの適切な組み合わせを選択することで、タンパク質の最適な分離が得られます。NuPAGEビス-トリスタンパク質ゲルには、4種類のポリアクリルアミド濃度があります:8%、10%、12%、および 4–12% のグラジエント。ゲルのサイズは、ミニ(8 cm×8 cm)またはミディ(8.7 cm×13.3 cm)の2種類があり、厚さは1.0 mm(ミニゲルおよびミディゲル)または1.5 mm(ミニゲルフォーマットのみ)です。また、NuPAGE Bis-Trisゲルには、複数のウェルフォーマットがあります。

NuPAGE Bis-Trisゲルは、変性ゲル電気泳動アプリケーション用に調製されています。最適なサンプル調製には、NuPAGE LDSサンプルバッファー(NP0007)およびNuPAGEサンプル還元剤(NP0004)をご使用ください。泳動バッファーにNuPAGE抗酸化剤(NP0005)を使用すると、泳動中のタンパク質の還元状態を維持し、バンドのシャープさを最大限に高めます。このゲルは、NuPAGE MES SDS Running Buffer(NP0002)を使用して泳動することで、少量のタンパク質の分離を促します。また、NuPAGE MOPS SDS Running Buffer(NP000102)を使用して中~大きいサイズのタンパク質を分離することができます。

タンパク質を膜に転写する場合は、Mini Blot Module(B1000)またはXCell II Blot Module(EI9051)を用いて、従来のウェットトランスファーにNuPAGE Transfer Buffer(NP00061)を使用することを推奨します。また、高速セミドライ転写にはInvitrogen Power Blotter、または高速ドライ転写にはiBlot 2 Gel転写装置(IB210010)を使用することも可能です。

For Research Use Only. Not for use in diagnostic procedures.
仕様
Gel Thickness1.0 mm
長さ(メートル法)8 cm
分離モード分子量
製品ラインNuPAGE
数量10ゲル/箱
推奨アプリケーション変性
サンプル充填量最大25 µL
品質保持期間12カ月
出荷条件室温
保存要件4–25 ℃ にて保管してください。冷凍不可。
幅(メートル法)8 cm
使用対象 (装置)Mini Gel Tank, XCell SureLock Mini-Cell
ゲル濃度12%
ゲルサイズミニ
ゲルタイプBis-Tris
分離範囲3.5~80 kDa
分離タイプ変性
ウェル10ウェル
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.

What does it mean when bands appear to be getting narrower (or "funneling") as they progress down a protein gel?

There may be too much beta-mercaptoethanol (BME), sample buffer salts, or dithiothreitol (DTT) in your samples. If the proteins are over-reduced, they can be negatively charged and actually repel each other across the lanes causing the bands to get narrower as they progress down the gel.

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

引用および参考文献 (6)

引用および参考文献
Abstract
The novel WD-repeat protein MORG1 acts as a molecular scaffold for HIF prolyl-hydroxylase 3 (PHD3).
Authors:Hopfer U, Hopfer H, Jablonski K, Stahl RA, Wolf G,
Journal:J Biol Chem
PubMed ID:16407229
'Hypoxia-inducible factor-1 (HIF-1), a transcriptional complex composed of an oxygen-sensitive alpha- and a beta-subunit, plays a pivotal role in cellular adaptation to low oxygen availability. Under normoxia, the alpha-subunit of HIF-1 is hydroxylated by a family of prolyl hydroxylases (PHDs) and consequently targeted for proteasomal degradation. Three different prolyl hydroxylases ... More
Nitric oxide-induced cellular stress and p53 activation in chronic inflammation.
Authors:Hofseth LJ, Saito S, Hussain SP, Espey MG, Miranda KM, Araki Y, Jhappan C, Higashimoto Y, He P, Linke SP, Quezado MM, Zurer I, Rotter V, Wink DA, Appella E, Harris CC,
Journal:Proc Natl Acad Sci U S A
PubMed ID:12518062
Free radical-induced cellular stress contributes to cancer during chronic inflammation. Here, we investigated mechanisms of p53 activation by the free radical, NO. NO from donor drugs induced both ataxia-telangiectasia mutated (ATM)- and ataxia-telangiectasia mutated and Rad3-related-dependent p53 posttranslational modifications, leading to an increase in p53 transcriptional targets and a G(2)M ... More
Inhibition of the human thioredoxin system. A molecular mechanism of mercury toxicity.
Authors:Carvalho CM, Chew EH, Hashemy SI, Lu J, Holmgren A,
Journal:J Biol Chem
PubMed ID:18321861
Mercury toxicity mediated by different forms of mercury is a major health problem; however, the molecular mechanisms underlying toxicity remain elusive. We analyzed the effects of mercuric chloride (HgCl(2)) and monomethylmercury (MeHg) on the proteins of the mammalian thioredoxin system, thioredoxin reductase (TrxR) and thioredoxin (Trx), and of the glutaredoxin ... More
Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: Spermine is converted to spermidine in vivo by the FMS1-amine oxidase.
Authors:Chattopadhyay MK, Tabor CW, Tabor H,
Journal:Proc Natl Acad Sci U S A
PubMed ID:14617780
In our earlier work we showed that either spermidine or spermine could support the growth of spe2Delta or spe3Delta polyamine-requiring mutants, but it was unclear whether the cells had a specific requirement for either of these amines. In the current work, we demonstrate that spermidine is specifically required for the ... More
Heat shock protein-70 expressed on the surface of cancer cells binds parathyroid hormone-related protein in vitro.
Authors:Grzesiak JJ, Smith KC, Chalberg C, Truong C, Burton DW, Deftos LJ, Bouvet M,
Journal:Endocrinology
PubMed ID:15878959
Recent studies have shown that the functions of PTH-related protein (PTHrP) and its derived peptides cannot be attributed solely to PTH/PTHrP receptor binding. The present study focused on the identification of other proteins that might bind PTHrP at the cell surface. Using affinity chromatography, we applied extracts of cell-surface biotinylated ... More