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.
- What is Ph.D.™ Phage Display?
- Which residues does Endoproteinase AspN cut?
- 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.
- Is there a simple way to remove Trypsin after protein cleavage?
- How does one do a Trypsin in-gel digest?
- 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?
- What is the Proteinase K activity in commonly used buffers?
- Ph.D.™ Peptide Display Cloning System
- Simultaneous Fluorescent Labeling of Proteins in Living Cells
- Intein-Mediated Protein Ligation IPL and Labeling with the IMPACT™ Kit
- Analysis of a Fusion Protein using the Protein Deglycosylation Mix II and Mass Spectrometry
- Enzymatic removal of N- and O-glycans using PNGase F or the Protein Deglycosylation Mix
- Using Glycosidases to Remove, Trim, or Modify Glycans on Therapeutic Proteins
Combating Neglected Diseases - a genomic approach to identify potential drug targets
Parasitic Infections in Humans
Understand the common types of parasitic infections in humans and why they are still increasing in tropical regions.
Applications of the Ph.D. Phage Display Peptide Libraries
- A monoclonal antibody for transcriptome-wide N6-methyladenosine analysis (2017)
- Crystal Structure of the 8 bp-Specific Restriction Enzyme SwaI (2015)
- NiCo21(DE3): A BL21(DE3) Derivative Designed for Expression and Purification of His-tagged Recombinant Protein (2015)
- Development of a Rapid Method for Genome Engineering in a Quest Towards Customized Protein Expression Strains (2015)
- Discovering the Maltose Binding Protein epitope tag for Escherichia coli expressed proteins (2018)
- Selection for proteins that overcome heatinduced lethality of ΔdegP strain (2018)
- Leith, E.M., O'Dell, W.B., Ke, N., McClung, C., Berkmen, M., Bergonzo, C., Brinson, R.G., Kelman, Z 2019. Characterization of the internal translation initiation region in monoclonal antibodies expressed in Escherichia coli J Biol Chem. 294(48), PubMedID: 31604819, DOI: 10.1074/jbc.RA119.011008
- Ke, Na; Berkmen, Mehmet; Ren, Guoping; 2017. A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo Nat Chem Biol. 13, PubMedID: 28628094, DOI: 10.1038/nchembio.2409
This product is covered by one or more patents, trademarks and/or copyrights owned or controlled by New England Biolabs, Inc (NEB).
While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.
For more information about commercial rights, please contact NEB's Global Business Development team at email@example.com.
This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.