Jule Precast Gels

BUFFER SYSTEM SELECTION

 

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LONG LIFE TRIS-GLYCINE GELS  12 MONTH SHELF LIFE

Long Life Tris-Glycine Gels run with standard 1X Tris-Glycine running buffer.

 

Denaturing or Non-Denaturing Gels, pH 7: They are similar to Laemmli Gels. These gels can be used for denatured or non-denatured proteins.   To run denatured proteins treat your sample with a denaturing sample buffer and use running buffer that contains SDS.  See proteins separated on Gels (Click here).

 

TRIS-GLYCINE GELS - Standard Laemmli-type gel buffer, 2 month shelf life

The Gel buffer is 0.375M Tris-HCl, pH 8.8.  Tris-Glycine Gels can be used for denaturing or non-denaturing samples.  Tris-Glycine Gels can purchased with or without SDS

 

Denaturing Gels (Contains SDS):  Gel buffer is 0.375M Tris-HCl, pH 8.8, 0.1 % SDS.  These Gels enable the proteins to be separated on the basis of size alone. The proteins are no longer active, since they are unfolded.  To run denatured proteins treat your sample with a denaturing sample buffer and use running buffer that contains SDS.  See proteins separated on Gels (Click here).

 

Non-Denaturing Gels (No SDS in Gel Buffer):  The Gel buffer is 0.375M Tris-HCl, pH 8.8   Non-Denaturing Gels are used for separating proteins in their Native State. Native means any of the following: 1) The structure of a protein as it exists in nature; 2) the structure of a protein as isolated, if it retains enzymatic activity; 3) the form of a protein that has no biological activity but possesses secondary structure. To run denatured proteins treat your sample with a denaturing sample buffer and use running buffer that contains SDS.    See proteins separated on Gels (Click here).

Tricine Gels:

Gel buffer is 1.0 M Tris-HCl, pH 8.45, 0.1 % SDS.  These Gels are used for separating proteins or peptides as small as 1,000 Daltons (1kD). Tricine in the running buffer migrates faster than Glycine and the smallest proteins, thereby enabling separation.  Use Tricine Gels for separating low molecular weight proteins (70,000 to 1,000 Daltons).  They can also be used for separating proteins from 212,000 to 1,000 Daltons depending upon the acrylamide gel concentration.  Tricine Gels use a different upper and lower running buffer (see Running Buffers) See proteins separated on Gels (Click here).  

TBE Gels, Non-Denaturing (for DNA, RNA, PCR product analysis, and proteins): The Gel buffer is 0.090 M Tris, 0.080 M Boric Acid, pH 8.3, 0.0026M EDTA.  These Gels are used for non-denaturing (native) protein analysis as described above under non-denaturing Tris-Glycine gels and non denaturing DNA and RNA analysis (double stranded). The applications for DNA, include but are not limited to, purification of DNA restriction fragments for cloning, PCR product analysis and purification, and gel mobility shift assays. TBE Gels are typically used for HDL and LDL separations.   These Gels use TBE Running Buffer.
TBE/UREA Gels, Denaturing: Same as TBE Gels, except Urea (7 molar) is added. These gels are used for single stranded DNA and RNA analysis.  The Urea is a denaturing agent that causes the DNA and RNA to become single-stranded by breaking the bonds that usually hold the DNA and RNA together.  The applications for this type of gel include: DNA size measurements and Southern Blot analysis, RNA size measurements and Northern Blot analysis, DNA foot printing (localizing of protein binding site on DNA or detection of DNA Binding proteins), RNA foot printing (location of site of RNA-binding proteins), and purification of oligonucleotides used for PCR and cDNA screening.  These Gels use TBE Running Buffer.

Tris Acetate Gels, Long life Gels (up to 8 months shelf life). Can be used to separate proteins from 240,000 to 14,000 Daltons. Available in single or gradient gel concentrations.

For high molecular weight proteins up to 500 kD, choose a low concentration gel, either single or gradient concentration.

Blue Native Gels: Blue Native Page was originally described by Schagger and von Jagow as a technique for the separation of enzymatically active membrane protein complexes under mild conditions.  In this variation of gel electrophoresis, the anionic dye, Coomassie Brilliant Blue, is added to the sample prior to loading and binds to protein complexes during electrophoresis under physiological conditions.  The technique has gained interest from researchers focused on functional proteomics in recent years, as it allows the study of protein-protein interactions, and the separation and analysis of very hydrophobic proteins, such as membrane proteins, their complexes, and even super complexes.

References:

1. Schagger, H. and Jagow, G. (1991) Blue Native electrophoresis for isolation of membrane protein complexes, Anal Biochem. 199, 223-231.   

 

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