Native SDS PAGE Kit

easy to implement Native SDS-PAGE method has retained the enzymatic activity of a number of enzymes tested, and has also maintained protein complexes in a bound state. This new technology will allow for multiple new applications in drug discovery, proteomics, protein therapeutics, and toxicology.

Contributors

Institute
University of Wisconsin-Milwaukee
Cat. #: 153814
Research Fields: Cell biology;Other
Product description: There is a great need for a robust method that combines the electrophoretic resolution of proteins with retention of their functional behavior. The laboratory of Dr. David Petering has devised a new method of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in which proteins can be well separated during electrophoresis as well as maintain their native 3-dimensional conformations and functional activity. This native SDS-PAGE method will allow for important new experiments to be conducted in the proteomic field and a better understanding of proteins such as isolation from the gel of native proteins for further analysis, direct in-gel assay of enzymatic activity, direct in-gel survey of binding activity of proteins with small molecules (e.g. drugs, toxic agents) and macromolecules (e.g. protein binding partners including antibodies, cognate DNA binding sites), and isolation of protein for subsequent mass spectral identification.In traditional SDS-PAGE the proteins are well separated but are denatured such that the structure and function are no longer adequately maintained for carrying out further functional assays. The current commercial alternative, known as native PAGE, enables researchers to maintain protein function and structure, but the technique leads to poor separation and smearing of protein during electrophoresis. Our easy to implement Native SDS-PAGE method has retained the enzymatic activity of a number of enzymes tested, and has also maintained protein complexes in a bound state. This new technology will allow for multiple new applications in drug discovery, proteomics, protein therapeutics, and toxicology.
Additional notes: Can be performed using commercial pre-casted gels. Simple technique and requires only one buffer system. Can retain the functional activity of proteins tested. Can retain binding of protein complexes. The neutral pH of the NSDS buffer system has an advantage over the high pH Tri-glycine system for separation of the pH sensitive proteins.
Storage conditions: RT
Shipping conditions: Dry Ice
Solubility: N/A
References:

Nowakowski et al. 2014. Metallomics. 6(5):1068-78. PMID: 24686569.

Native SDS-PAGE: high resolution electrophoretic separation of proteins with retention of native properties including bound metal ions.

Related Tools for Small molecules

Cat. # Tool Name
151712 CDK7 inhibitor BS-181 Small Molecule (Tool Compound) Key Info View Tool
151880 AKR1C3 inhibitor CRT0093964 Small Molecule (Tool Compound) Key Info View Tool
151889 DNA-PK inhibitor NU7441 Small Molecule (Tool Compound) Key Info View Tool
152433 HDAC2/3 inhibitor MI-192 Small Molecule (Tool Compound) Key Info View Tool
152741 Platinum trimethyl Luminophore Small Molecule (Tool Compound) Key Info View Tool

Tool enquiry

Please ensure you use your organisation email address rather than personal where possible, as this helps us locate your organisation in our system faster.

Please note we may take up to three days to respond to your enquiry.

CancerTools.org uses the contact information provided to respond to you about our research tools and service. For more information please review our privacy policy.