NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm

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NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm

Citations & References (4)

Invitrogen™

NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm

Name: NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm
SKU: NP0330BOX

Invitrogen NuPAGE ビス－トリスタンパク質ゲルはプレキャストポリアクリルアミドゲルであり、高分解能とサンプルの完全性で、分子量の広いタンパク質分離を実現します。

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製品番号（カタログ番号）	ウェル	Gel Thickness	数量
NP0330BOX	IPGウェル	1.0 mm	10ゲル／箱
NP0321BOX	10ウェル	1.0 mm	10ゲル／箱
NP0321PK2	10ウェル	1.0 mm	2ゲル／箱
NP0322BOX	12ウェル	1.0 mm	10ゲル／箱
NP0322PK2	12ウェル	1.0 mm	2ゲル／箱
NP0323BOX	15ウェル	1.0 mm	10ゲル／箱
NP0323PK2	15ウェル	1.0 mm	2ゲル／箱
NP0324BOX	1ウェル	1.0 mm	10ゲル／箱
NP0326BOX	2Dウェル	1.0 mm	10ゲル／箱
NP0327BOX	9ウェル	1.0 mm	10ゲル／箱
NP0329BOX	17ウェル	1.0 mm	10ゲル／箱
NP0329PK2	17ウェル	1.0 mm	2ゲル／箱
NP0335BOX	10ウェル	1.5 mm	10ゲル／箱
NP0335PK2	10ウェル	1.5 mm	2ゲル／箱
NP0336BOX	15ウェル	1.5 mm	10ゲル／箱
NP0336PK2	15ウェル	1.5 mm	2ゲル／箱

16 オプション

製品番号（カタログ番号） NP0330BOX

価格（JPY）

27,500

Each

お問い合わせください ›

ウェル:

IPGウェル

Gel Thickness:

1.0 mm

数量:

10ゲル／箱

Invitrogen NuPAGE ビス－トリスタンパク質ゲルはプレキャストポリアクリルアミドゲルであり、高分解能とサンプルの完全性で、分子量の広いタンパク質分離を実現します。これらのプレキャストゲルは、タンパク質の完全性が重要なアプリケーションに最適です。従来のトリス-グリシンゲルとは異なり、NuPAGEビス-トリスゲルのpH環境は中性であるため、タンパク質修飾を最小限に抑えます。NuPAGE ビス－トリスゲルは、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術用に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（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）8 cm

分離モード分子量

製品ラインNuPAGE、ZOOM

数量10ゲル／箱

サンプル充填量7 cmストリップ

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4 ～ 12%

ゲルサイズミニ

ゲルタイプBis-Tris

分離範囲3.5～260 kDa

分離タイプ変性

ウェルIPG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 may cause streaking on the 2nd dimension gel after IEF?

There are several reasons why streaking may occur.

(1) Sample is not completely solubilized prior to application.

(2) Sample is poorly soluble in rehydration solution.

(3) Non-protein impurities in the sample can interfere with IEF, causing horizontal streaking in the final 2-D result, particularly toward the acidic side of the gel.

(4) Ionic impurities are present in sample.

(5) Ionic detergent is present in sample.

(6) Sample load is too high.

(7) Underfocusing. Focusing time was not long enough to achieve steady state focusing.

(8) Overfocusing. Extended focusing times (over 100,000 Vh) may result in electroendosmotic water and protein movement, which can produce horizontal smearing.

What should be done?

(1) Be sure that the sample is completely and stably solubilized. Note: Repeated precipitation-resolubilization cycles produce or increase horizontal streaking.

(2) Increase the concentration of the solubilizing components in the rehydration solution.

(3) Modify sample preparation to limit these contaminants or dialyze protein.

(4) Reduce salt concentration to below 10 mM by dilution or desalt the sample by dialysis. Precipitation with TCA and acetone and subsequent resuspension is another effective desalting technique that removes lipids, nucleotides and other small molecules.
Note: Specific and non-specific losses of proteins can occur with dialysis, gel chromatography, and precipitation/resuspension of samples. If the sample preparation cannot be modified, the effect of ionic impurities can be reduced by modifying the IEF protocol. Limit the voltage to 100-150 V for 2 hours, then resume a normal voltage step program. This pre-step allows the ions in the sample to move to the ends of the IPG strip.

(5) If the ionic detergent SDS is used in sample preparation, the final concentration must not exceed 0.25% after dilution into the rehydration solution. Additionally, the concentration of the non-ionic detergent present must be at least 8 times higher than the concentration of any ionic detergent to ensure complete removal of SDS from the proteins.

(6) Extend focusing time. Load less sample.

(7) Prolong focusing time.

(8) Reduce focusing time.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

View all NuPAGE™ Bis-Tris Mini Protein Gels, 4–12%, 1.0–1.5 mm FAQs

引用および参考文献 (4)

引用および参考文献

Abstract

Sero-epidemiology as a tool to screen populations for exposure to Mycobacterium ulcerans.

Authors:Yeboah-Manu D, Röltgen K, Opare W, Asan-Ampah K, Quenin-Fosu K, Asante-Poku A, Ampadu E, Fyfe J, Koram K, Ahorlu C, Pluschke G,

Journal:PLoS Negl Trop Dis

PubMed ID:22253937

'Previous analyses of sera from a limited number of Ghanaian Buruli ulcer (BU) patients, their household contacts, individuals living in BU non-endemic regions as well as European controls have indicated that antibody responses to the M. ulcerans 18 kDa small heat shock protein (shsp) reflect exposure to this pathogen. Here, ... More

Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease.

Authors:Zheng L, Nukuna B, Brennan ML, Sun M, Goormastic M, Settle M, Schmitt D, Fu X, Thomson L, Fox PL, Ischiropoulos H, Smith JD, Kinter M, Hazen SL,

Journal:J Clin Invest

PubMed ID:15314690

In recent studies we demonstrated that systemic levels of protein-bound nitrotyrosine (NO(2)Tyr) and myeloperoxidase (MPO), a protein that catalyzes generation of nitrating oxidants, serve as independent predictors of atherosclerotic risk, burden, and incident cardiac events. We now show both that apolipoprotein A-I (apoA-I), the primary protein constituent of HDL, is ... More

Akt-mediated valosin-containing protein 97 phosphorylation regulates its association with ubiquitinated proteins.

Authors:Klein JB, Barati MT, Wu R, Gozal D, Sachleben LR, Kausar H, Trent JO, Gozal E, Rane MJ,

Journal:J Biol Chem

PubMed ID:16027165

Hypoxia is a common environmental stress that influences signaling pathways and cell function. Previous studies from our laboratory have identified significant differences in cellular responses to sustained or intermittent hypoxia with the latter proving more cytotoxic. We hypothesized that differences in susceptibility of neurons to intermittent (IH) and sustained hypoxia ... More

Epstein-Barr virus protein kinase BGLF4 is a virion tegument protein that dissociates from virions in a phosphorylation-dependent process and phosphorylates the viral immediate-early protein BZLF1.

Authors:Asai R, Kato A, Kato K, Kanamori-Koyama M, Sugimoto K, Sairenji T, Nishiyama Y, Kawaguchi Y,

Journal:J Virol

PubMed ID:16698993

Epstein-Barr virus (EBV) BGLF4 is a viral protein kinase that is expressed in the lytic phase of infection and is packaged in virions. We report here that BGLF4 is a tegument protein that dissociates from the virion in a phosphorylation-dependent process. We also present evidence that BGLF4 interacts with and ... More