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Novex™ Tris-Glycine SDS Sample Buffer (2X)
Novex™ Tris-Glycine SDS Sample Buffer (2X)
Novex™ Tris-Glycine SDS Sample Buffer (2X)
인용 및 참조 문헌 (1)
Invitrogen™

Novex™ Tris-Glycine SDS Sample Buffer (2X)

Novex Tris-Glycine SDS Sample Buffer (2X) is used to prepare protein samples for denaturing gel electrophoresis using Tris-Glycine gels. It자세히 알아보기
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카탈로그 번호수량
LC267620 mL
카탈로그 번호 LC2676
제품 가격(KRW)
42,000
Online offer
Ends: 30-Jun-2026
47,000
할인액 5,000 (11%)
Each
수량:
20 mL
제품 가격(KRW)
42,000
Online offer
Ends: 30-Jun-2026
47,000
할인액 5,000 (11%)
Each
Novex Tris-Glycine SDS Sample Buffer (2X) is used to prepare protein samples for denaturing gel electrophoresis using Tris-Glycine gels. It has a pH of 6.8 and contains bromophenol blue as a tracking dye.

See all available buffers and reagents available for SDS-PAGE

To use: Heat the sample in a 1X dilution (reduced or non-reduced) at 85°C for 2–5 minutes for optimal results. Heating samples at 100°C in SDS-containing buffers results in proteolysis.
For Research Use Only. Not for use in diagnostic procedures.
사양
화학물질 이름 또는 재질Sample Loading Buffer
권장 스토리지Tris-Glycine Sample Buffer (2X) containing sodium dodecyl sulfate (SDS) at pH 6.8 with bromophenol blue.

Store at 2°C to 8°C.

농도2X
물리적 형태Liquid
제품라인Novex
수량20 mL
Unit SizeEach

자주 묻는 질문(FAQ)

Where do I find buffer recipes for your precast protein gels?

The formulations of buffers for our precast protein gels can be found at this link: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-gel-electrophoresis/protein-electrophoresis-buffers-reagents.html

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

What is the recipe for traditional Laemmli Buffer?

The Laemmli buffer or 2X SDS Buffer is composed of the following: 100 mM Tris HCl , pH 6.8, 200 mM dithiothreitol, 4% SDS, 0.2% bromophenol blue, 20% glycerol. 2X SDS gel loading buffer lacking dithiothreitol can be stored at room temperature. Dithiothreitol should then be added, just before use.

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

If a Tricine gel is accidentally run with buffers used in the Tris-Glycine system, what will happen and why?

If the Tricine gel is run with Tris-Glycine sample buffer, the bands will behave abnormally and resolve poorly. If the Tricine gel is accidentally run with Tris-Glycine running buffer, the gel will take longer to run and the resolution, especially for smaller proteins, will be worse than when the proteins are run on a Tris-Glycine gel with Tris-Glycine buffers. This is due to a combination of increase in stack area size (glycine is a slower ion than Tricine) and the higher ionic strength of the Tricine gel.

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

Why is LDS (lithium dodecyl sulfate) used in the 4X NuPAGE sample buffer instead of SDS?

SDS in a 4X sample buffer concentrate tends to precipitate from solution and to make the solution viscous and difficult to pipette. The LDS is much more soluble.

Find additional tips, troubleshooting help, and resources within our Protein Gel 1D Electrophoresis Support Center.

Can I use CTAB rather than SDS in my sample buffer?

No, CTAB will not work with any of our gels except for the NuPAGE Tris-Acetate gels. To use CTAB, you would need to use a running buffer of 50 mM acetic acid and 50 mM beta-alanine in equal concentrations. You would also need to switch the electrodes. Since CTAB is a cationic detergent, this would establish conditions for running a basic protein towards the anode (into the gel).

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

인용 및 참조 문헌 (1)

인용 및 참조 문헌
Abstract
Identification of components of protein complexes using a fluorescent photo-cross-linker and mass spectrometry.
Authors: Wine Robert N; Dial John M; Tomer Kenneth B; Borchers Christoph H;
Journal:Anal Chem
PubMed ID:12033289
'This study describes a novel method for improving the specific recognition, detection, and identification of proteins involved in multiprotein complexes. The method is based on a combination of coimmunoprecipitation, chemical cross-linking, and specific fluorescent tagging of protein components in close association with one another. Specific fluorescent tagging of the protein ... More