Not only are proteins a major structural component of living systems, they can also be effector molecules whose states determine downstream activities. Therefore, studying the protein complement within a cell can reveal the mechanisms behind many of the cell’s responses to its environment. Given the vast number of applications for protein analysis, several tools and methods for its study exist; determining the correct method for your application is paramount to success.
Protein Analysis & Tools includes these areas of focus:
FAQs for Protein Analysis & Tools
- What is Ph.D.™ Phage Display?
- Which residues does Endoproteinase AspN cut?
- What is the Proteinase K activity in commonly used buffers?
- I have a very low concentration of protein and would prefer not to denature as a separate step with buffer exchange before digestion. What denaturants can he use in the Trypsin reaction itself?
- How does one do a Trypsin in-gel digest?
- Is there a simple way to remove Trypsin after protein cleavage?
- Are there any amino acid residues that inhibit or reduce the efficiency of digestion of glutamate residues in a peptide sequence with Endoproteinase GluC? The site I want to digest has a glutamate residue followed by a proline residue and some enzymes are inhibited by the presence of a proline after the hydrolysis site.
Protocols for Protein Analysis & Tools
Application Notes Protein Analysis & Tools
Applications of the Ph.D. Phage Display Peptide Libraries
Combating Neglected Diseases - a genomic approach to identify potential drug targets
Parasitic Infections in Humans