Differences Between SDS PAGE and Native PAGE

The native page vs SDS page is discussed in the following table:

Criteria

SDS PAGE

Native PAGE

Description

A technique that separates the proteins based on their molecular weight or mass

A technique that separates the proteins based on their size, charge, and shape

Feature of Gel

Denaturing gel is used

Non-denaturing gel is used

Presence of SDS in Gel

SDS is present

SDS is absent

Buffer composition

The buffer has a reducing agent like DTT or BME

The buffer has no reducing agent

Sample preparation

Protein samples are heated

Protein samples are not heated

Separation criteria

Proteins are separated based on molecular weight

Proteins are separated based on molecular size and overall charge

Net charge on proteins

Always negative

Can either be positive or negative

Temperature

SDS PAGE is run at room temperature

Native PAGE is run at 4oC

Protein stability

Unstable

Stable

State of protein

Denatured

Native conformation or folded state

Protein recovery

Cannot be recovered post separation

Can be recovered post separation

Protein function

Proteins lose their function

Proteins retain their function

Used for

To detect presence of a protein; determine molecular weight (MW) of a protein; check protein expression etc.

To study the structure, subunit composition and function of proteins; purify proteins from a mixture in native form.

Ease of use

Easier, frequently used

Comparatively difficult, infrequent usage

Differences between SDS PAGE and Native PAGE

The difference between SDS-PAGE and native PAGE lies in how proteins are separated in the polyacrylamide gel. In SDS-PAGE, the migration rate of the protein is determined by its molecular weight only, whereas in native PAGE, the migration rate depends on both the size and overall charge of the protein. In this article, we will study the process of SDS PAGE and Native PAGE as well as the similarities and differences between SDS-PAGE and native PAGE.

Table of Content

  • Differences Between SDS PAGE and Native PAGE
  • What is SDS PAGE?
  • What is Native PAGE?
  • Similarities between SDS PAGE and Native PAGE
  • Conclusion – Differences Between SDS PAGE and Native PAGE
  • FAQs on SDS PAGE and Native PAGE

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Differences Between SDS PAGE and Native PAGE

The native page vs SDS page is discussed in the following table:...

What is SDS PAGE?

SDS-PAGE full form is Sodium dodecyl-sulfate polyacrylamide gel electrophoresis. It is a polyacrylamide gel electrophoresis technique, widely used in molecular biology. This technique is used to separate proteins by their molecular weight. It was developed by Ulrich K. Laemmli....

What is Native PAGE?

Native PAGE electrophoresis is another polyacrylamide gel electrophoresis technique, used in molecular biology to study the composition, native structure and function of the proteins. This technique separates the protein molecules based on the size and overall charge of the protein. It was developed by Ornstein and Davis. Since SDS is not used as a denaturing agent in the gel, the protein molecules retain their folded state and functionality. The buffers used in SDS PAGE do not contain any denaturing and reducing agents....

Similarities between SDS PAGE and Native PAGE

Some similarities between SDS PAGE and Native PAGE are:...

Conclusion – Differences Between SDS PAGE and Native PAGE

In conclusion, SDS-PAGE and Native PAGE are two distinct techniques in molecular biology for protein separation. This article discusses the comparision between SDS PAGE and Native PAGE. SDS-PAGE separates proteins by molecular weight in denaturing conditions. Native PAGE separates proteins based on size and charge under non-denaturing conditions. It also preserves native conformation and functionality of the proteins. SDS-PAGE is used for protein detection and molecular weight determination. Native PAGE is used for studying protein structure, composition, and function....

FAQs on SDS PAGE and Native PAGE

Why is SDS not used in Native PAGE?...