NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm
Run Invitrogen Mini Protein Gels in Bio-Rad's Mini-PROTEAN® Tetra Cell. Click here for more information.
NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm
NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm
NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm
NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm
Invitrogen™

NuPAGE™ Bis-Tris Mini Protein Gels, 10%, 1.0–1.5 mm

Invitrogen NuPAGE Bis-Tris protein gels are precast polyacrylamide gels that provide broad molecular weight protein separation with high resolution and sample integrity. These precast gels are ideal for applications where protein integrity is crucial.
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카탈로그 번호Gel Thickness수량
NP0315BOX10-well1.5 mm10 gels (1 box)
NP0301BOX10-well1.0 mm10 gels (1 box)
NP0301PK210-well1.0 mm2 gels (1 box)
NP0302BOX12-well1.0 mm10 gels (1 box)
NP0302PK212-well1.0 mm2 gels (1 box)
NP0303BOX15-well1.0 mm10 gels (1 box)
NP0304BOX1-well1.0 mm10 gels (1 box)
NP0306BOX2D-well1.0 mm10 gels (1 box)
NP0307BOX9-well1.0 mm10 gels (1 box)
NP0316BOX15-well1.5 mm10 gels (1 box)
카탈로그 번호 NP0315BOX
제품 가격(KRW)
291,000
Each
카트에 추가하기
웰:
10-well
Gel Thickness:
1.5 mm
수량:
10 gels (1 box)
제품 가격(KRW)
291,000
Each
카트에 추가하기
Invitrogen NuPAGE Bis-Tris protein gels are precast polyacrylamide gels that provide broad molecular weight protein separation with high resolution and sample integrity. These precast gels are ideal for applications where protein integrity is crucial. Unlike traditional Tris-glycine gels, NuPAGE Bis-Tris gels have a neutral pH environment that minimizes protein modifications. Use NuPAGE Bis-Tris gels for preparing proteins for sequencing, mass spectrometry, and any other techniques where protein integrity is important.

Features of NuPAGE Bis-Tris gels:
Better protein integrity—optimized sample preparation process preserves your proteins
Wide ranges of molecular weight separation—select the right gel and running buffer to get the optimal separation of your proteins
Faster run times—get separation of your proteins in as little as 35 minutes
Longer shelf life—NuPAGE Bis-Tris gels can be stored for at least 12 months at room temperature

Choose the right NuPAGE Bis-Tris gel for your protein separation
Obtain optimal separation of your proteins by choosing the right combination of gel and running buffer. NuPAGE Bis-Tris protein gels come in four polyacrylamide concentrations: 8%, 10%, 12%, and a 4–12% gradient. Gels come in two sizes: mini (8 cm x 8 cm) or midi (8.7 cm x 13.3 cm) and either 1.0 mm (mini and midi gels) or 1.5 mm (mini gel format only) in thickness. NuPAGE Bis-Tris gels also come in multiple well formats.

NuPAGE Bis-Tris gels are formulated for denaturing gel electrophoresis applications. For optimal sample preparation, use the NuPAGE LDS Sample Buffer (NP0007) and NuPAGE Sample Reducing Agent (NP0004). Use NuPAGE Antioxidant (NP0005) in the running buffer to maintain the reduced state of the proteins during the run and to allow maximum band sharpness. The gels can be run using NuPAGE MES SDS Running Buffer (NP0002) to better resolve small proteins or NuPAGE MOPS SDS Running Buffer (NP000102) to resolve medium- to large-size proteins.

For transfer of proteins to a membrane, we recommend using NuPAGE Transfer Buffer (NP00061) for traditional wet transfer using the Mini Blot Module (B1000) or XCell II Blot Module (EI9051). Alternatively, rapid semi-dry transfer can be done using the Invitrogen Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device (IB210010).

For Research Use Only. Not for use in diagnostic procedures.
사양
Gel Thickness1.5 mm
길이(미터법)8 cm
분리 모드Molecular Weight
제품라인NuPAGE
수량10 gels (1 box)
권장 애플리케이션Denaturing
샘플 로딩 부피Up to 37 μL
유통 기한12 Months
배송 조건Room Temperature
보관 요구 사항Store at 4–25°C. Do not freeze.
폭(미터법)8 cm
용도 (장비)Mini Gel Tank, XCell SureLock Mini-Cell
젤 비율10%
젤 크기Mini
젤 유형Bis-Tris
분리 범위3.5 to 260 kDa
분리 유형Denaturing
10-well
Unit SizeEach

자주 묻는 질문(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.

인용 및 참조 문헌 (6)

인용 및 참조 문헌
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
Differentiation of mouse embryonic stem cells following RNAi-mediated silencing of OCT4 and Nanog.
Authors:Hough SR, Clements I, Welch PJ, Wiederholt KA,
Journal:Stem Cells
PubMed ID:16456133
RNAi holds great promise as a tool to study the basic biology of stem cells or to direct differentiation in a specific manner. Barriers to achieving efficient and specific gene silencing in RNAi experiments include limitations in transfection efficiency and in the efficacy and specificity of RNAi silencing effectors. Here, ... More
Oligomerization of the fifth transmembrane domain from the adenosine A2A receptor.
Authors:Thévenin D, Lazarova T, Roberts MF, Robinson CR,
Journal:Protein Sci
PubMed ID:15987888
The human adenosine A2A receptor (A(2A)R) belongs to one of the largest family of membrane proteins, the G-protein coupled receptors (GPCRs), characterized by seven transmembrane (TM) helices. Little is known about the determinants of their structures, folding, assembly, activation mechanisms, and oligomeric states. Previous studies in our group showed that ... More
A regulatory light chain of ciliary outer arm dynein in Tetrahymena thermophila.
Authors:Christensen ST, Guerra C, Wada Y, Valentin T, Angeletti RH, Satir P, Hamasaki T,
Journal:J Biol Chem
PubMed ID:11274140
Ciliary beat frequency is primarily regulated by outer arm dyneins (22 S dynein). Chilcote and Johnson (Chilcote, T. J., and Johnson, K. A. (1990) J. Biol. Chem. 256, 17257-17266) previously studied isolated Tetrahymena 22 S dynein, identifying a protein p34, which showed cAMP-dependent phosphorylation. Here, we characterize the molecular biochemistry ... More
Identification and expression of immunogenic proteins of a disease-associated marine turtle herpesvirus.
Authors:Coberley SS, Condit RC, Herbst LH, Klein PA,
Journal:J Virol
PubMed ID:12239336
Herpesviruses are associated with several diseases of marine turtles, including lung-eye-trachea disease (LETD) and fibropapillomatosis. Two approaches were used to identify immunodominant antigens of LETV, the LETD-associated herpesvirus. The first approach targeted glycoprotein B, which is known to be immunogenic and neutralizing in other species. The second strategy identified LETV ... More