NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
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NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm
Invitrogen™

NuPAGE™ Tris-Acetate Mini Protein Gels, 3 to 8%, 1.0–1.5 mm

Invitrogen NuPAGE Tris-Acetateタンパク質ゲルは、高分子量タンパク質の優れた分離を実現します。このゲルは高性能のポリアクリルアミドゲルで、従来のLaemmliシステムの変性条件や天然条件をシミュレートします。
製品番号(カタログ番号)ウェルGel Thickness数量
EA0375BOX10ウェル1.0 mm10ゲル/箱
EA0375PK210ウェル1.0 mm2ゲル/箱
EA03752BOX12ウェル1.0 mm10ゲル/箱
EA03752PK212ウェル1.0 mm2ゲル/箱
EA03755BOX15ウェル1.0 mm10ゲル/箱
EA0378BOX10ウェル1.5 mm10ゲル/箱
EA03785BOX15ウェル1.5 mm10ゲル/箱
製品番号(カタログ番号) EA0375BOX
価格(JPY)
31,000
Each
お問い合わせください ›
ウェル:
10ウェル
Gel Thickness:
1.0 mm
数量:
10ゲル/箱
Invitrogen NuPAGE Tris-Acetateタンパク質ゲルは、高分子量タンパク質の優れた分離を実現します。このゲルは高性能のポリアクリルアミドゲルで、従来のLaemmliシステムの変性条件や天然条件をシミュレートします。独自のバッファー組成により、電気泳動中に低い有効pHを維持するため、従来のTris-glycine SDS-PAGEゲルよりも優れた高分子量タンパク質の分離を実現します。

NuPAGE Tris-Acetateゲルの特長:
高分解能—ゲルは高分子量タンパク質の最適な分離をもたらします
より優れたタンパク質の完全性—サンプル調製プロセスをタンパク質の保存に役立つように最適化
長期の品質保持期間—8カ月以上保存が可能

タンパク質分離に最適なNuPAGE Tris-Acetateゲルの選択
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、高分子量のタンパク質が得られます。NuPAGE Tris-Acetateタンパク質ゲルは、7%濃度のポリアクリルアミド、3~8%のグラジエントで提供します。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 Tris-Acetateゲルには、複数のウェルフォーマットがあります。ミニゲルはXCell SureLockミニセル(EI0001)、またはミニゲルタンク(A25977)を使用して泳動できます。Midiゲルは、XCell4 SureLock Midi-Cell(WR01000)、またはBio-Rad Criterion™ Cellのアダプター(WA0999)を使って簡便に実行することができます。

タンパク質をネイティブまたは変性した状態で測定します
NuPAGE Tris-Acetateタンパク質ゲルは、SDSを含んでいないため、ネイティブまたは変性タンパク質の分離に使用することができます。変性タンパク質には、NuPAGE LDSサンプルバッファー(NP0007)およびNuPAGE Tris-Acetate SDS泳動バッファー(LA0041)の使用をお勧めします。天然タンパク質の場合、Novex Tris-Glycineネイティブサンプルバッファー(LC2673)およびNovex Tris-Glycineネイティブ泳動バッファー(LC2672)の使用をお勧めします。

タンパク質を膜に転写する場合は、XCell IIブロットモジュール(EI9051)またはミニブロットモジュール(B1000)を用いた従来のウェット転写用に、NuPAGE転写バッファー(NP00061)の使用をお勧めします。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(IB21001)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)13 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、天然
サンプル充填量最大25 µL
品質保持期間8カ月
出荷条件湿氷
保存要件2~8℃にて保存してください。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3 ~ 8%
ゲルサイズミニ
ゲルタイプトリス-アセテート
分離範囲36~500 kDa
分離タイプ変性、天然
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 (7)

引用および参考文献
Abstract
Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein.
Authors: Denning G; Jamieson L; Maquat L E; Thompson E A; Fields A P;
Journal:J Biol Chem
PubMed ID:11331269
'We have cloned and characterized a new member of the phosphatidylinositol kinase (PIK)-related kinase family. This gene, which we term human SMG-1 (hSMG-1), is orthologous to Caenorhabditis elegans SMG-1, a protein that functions in nonsense-mediated mRNA decay (NMD). cDNA sequencing revealed that hSMG-1 encodes a protein of 3031 amino acids ... More
Multimerization of the ligand binding domains of cyclic nucleotide-gated channels.
Authors: Matulef Kimberly; Zagotta William;
Journal:Neuron
PubMed ID:12367509
Cyclic nucleotide-gated (CNG) channels comprise four subunits and are activated by the direct binding of cyclic nucleotide to an intracellular domain on each subunit. This ligand binding domain is thought to contain a beta roll followed by two alpha helices, designated the B and C helices. To examine the quaternary ... More
Dismantling of cadherin-mediated cell-cell contacts modulates smooth muscle cell proliferation.
Authors:Uglow EB, Slater S, Sala-Newby GB, Aguilera-Garcia CM, Angelini GD, Newby AC, George SJ,
Journal:Circ Res
PubMed ID:12775583
Proliferation of vascular smooth muscle cells (VSMCs) contributes to intimal thickening during atherosclerosis and restenosis. The cadherins are transmembrane proteins, which form cell-cell contacts and may regulate VSMC proliferation. In this study, N-cadherin protein concentration was significantly reduced by stimulation of proliferation with fetal calf serum (FCS) and platelet-derived growth ... More
The cytoplasmic tail of L-selectin interacts with members of the Ezrin-Radixin-Moesin (ERM) family of proteins: cell activation-dependent binding of Moesin but not Ezrin.
Authors:Ivetic A, Deka J, Ridley A, Ager A,
Journal:J Biol Chem
PubMed ID:11706008
L-selectin regulates the recruitment of naive lymphocytes from the bloodstream to secondary lymphoid organs, mediating their initial capture and subsequent rolling along high endothelial cell surface-expressed ligands in peripheral lymph nodes. In vivo, distribution of L-selectin and cell surface levels determine the tethering efficiency and rolling velocity of leukocytes, respectively. ... More
The 'involution' of mannose-binding lectin.
Authors:Seyfarth J, Garred P, Madsen HO,
Journal:Hum Mol Genet
PubMed ID:16115813
Mannose-binding lectin (MBL) acts as a serum opsonin in innate immune defense and induces complement activation by the lectin pathway. In humans, low levels of functional serum MBL are caused by the dominant action of three single nucleotide substitutions in exon 1 that disrupt the glycine-rich backbone structure of the ... More