News and Announcements
AthenaES Expands Specialty Proteins Product Line to Include GFPs, Luciferases, and Bacterial Esterases
Baltimore, MD. January 1, 2007-
AthenaES has recently expanded its specialty protein portfolio
with the addition of bacterial esterases, green fluorescent
proteins, and luciferases.
Athena?s green fluorescent proteins and luciferases include
Gaussia luciferase, Renilla mullerei luciferase, Renilla
reniformis green fluorescent protein, and Ptilosarcus green
fluorescent protein. GFPs and luciferases have proven to aid
significantly as tags in assays where low limits of detection
are critical; their high quantum yields make them particularly
useful in immunoassays. Gaussia luciferase and Renilla luciferase
are up to 1,000 times brighter than Firefly luciferase and are
ATP-independent, requiring only coelenterazine and O2 as substrates.
The Gaussia luciferase is supplied pre-biotinylated for direct
use in streptavidin/avidin based immunoassays. Athena?s GFPs and
luciferases are available in milligram and microgram quantities.
In addition, AthenaES now offers three bacterial esterases:
LypA, TesA, and VlpA. Employing an array of techniques to identify
esterase/lipase activity for industrial processes, an in-house
microbial collection of psychrophilic microbes was used to screen
for specific esterase/lipase activities. Two marine bacteria yielded
esterase/lipase genes encoding LypA (V. cholera) and VlpA (arctic-
derived Vibrio sp.). Cold-tolerant bacterial esterases and lipases
have the property of a more flexible structure which allows the
enzymes to accommodate a broad range of substrates and often to be
more solvent tolerant, properties that make these types of enzymes
ideal for the chemical modification of pharmacophore molecules.
LypA and VlpA have been shown to have a broad spectrum of substrate
activity, reacting with ester bonds in compounds with short and long
aliphatic chains as well as heterocyclic rings. VlpA exhibits
tolerance to solvents by retaining its catalytic activity in buffer-