EZQ™ Protein Quantitation Kit - Citations

EZQ™ Protein Quantitation Kit - Citations

View additional product information for EZQ™ Protein Quantitation Kit - Citations (R33200)

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Citations & References
Abstract
Induced paternal effects mimic cytoplasmic incompatibility in Drosophila.
AuthorsClark ME, Heath BD, Anderson CL, Karr TL
JournalGenetics
PubMed ID16489228
'Wolbachia is an intracellular microbe found in a wide diversity of arthropod and filarial nematode hosts. In arthropods these common bacteria are reproductive parasites that manipulate central elements of their host''s reproduction to increase their own maternal transmission in one of several ways. Cytoplasmic incompatibility (CI) is one such manipulation ... More
A novel approach to tag and identify geranylgeranylated proteins.
AuthorsChan LN, Hart C, Guo L, Nyberg T, Davies BS, Fong LG, Young SG, Agnew BJ, Tamanoi F,
JournalElectrophoresis
PubMed ID19784953
A recently developed proteomic strategy, the
Gamma-secretase is a functional component of phagosomes.
AuthorsJutras I, Laplante A, Boulais J, Brunet S, Thinakaran G, Desjardins M
JournalJ Biol Chem
PubMed ID16103123
Gamma-secretase is a high molecular mass protein complex that catalyzes the intramembrane cleavage of its protein substrates. Two proteins involved in phagocytosis, CD44 and the low density lipoprotein receptor-related protein, are gamma-secretase substrates, suggesting that this complex might regulate some aspects of phagocytosis. Our results indicate that the four components ... More
Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases.
AuthorsLemberg MK, Menendez J, Misik A, Garcia M, Koth CM, Freeman M
JournalEMBO J
PubMed ID15616571
Intramembrane proteases have the unusual property of cleaving peptide bonds within the lipid bilayer, an environment not obviously suited to a water-requiring hydrolysis reaction. These enzymes include site-2 protease, gamma-secretase/presenilin, signal peptide peptidase and the rhomboids, and they have a wide range of cellular functions. All have multiple transmembrane domains ... More
A rapid solid-phase fluorescence-based protein assay for quantitation of protein electrophoresis samples containing detergents, chaotropes, dyes, and reducing agents.
AuthorsAgnew BJ, Murray D, Patton WF
JournalElectrophoresis
PubMed ID15300765
A new solid-phase, fluorescence-based protein assay was developed that quantifies proteins in the presence of detergents, urea and reducing agents (one-dimensional sodium dodecyl sulfate (1-D SDS) lysis buffers and urea isoelectric focusing (IEF) buffers). A specially designed 96-well microplate facilitates application of protein samples to the assay paper and allows ... More
Combining microscale solution-phase isoelectric focusing with Multiplexed Proteomics dye staining to analyze protein post-translational modifications.
AuthorsSchulenberg B, Patton WF
JournalElectrophoresis
PubMed ID15300774
Previously, a strategy for rapidly identifying mitochondrial phosphoproteins was presented that involves prefractionating multisubunit complexes by sucrose gradient centrifugation, followed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and selective staining of phosphoproteins and total protein with fluorescent dyes [1]. Though suitable for evaluating the mitochondrial proteome, which consists of numerous ... More
Enhanced detergent extraction for analysis of membrane proteomes by two-dimensional gel electrophoresis.
AuthorsChurchward MA, Butt RH, Lang JC, Hsu KK, Coorssen JR
JournalProteome Sci
PubMed ID15941475
BACKGROUND: The analysis of hydrophobic membrane proteins by two-dimensional gel electrophoresis has long been hampered by the concept of inherent difficulty due to solubility issues. We have optimized extraction protocols by varying the detergent composition of the solubilization buffer with a variety of commercially available non-ionic and zwitterionic detergents and ... More