产品名称
Corning® 384孔微孔板,低边, NBS™ (non-binding surface), black polystyrene, non-sterile, lid: no, pack of 25
material
black polystyrene
clear bottom
flat wells
polystyrene
sterility
non-sterile
feature
lid: no
skirt
plate format: low flange
packaging
case of 100 ea
pack of 25
manufacturer/tradename
Corning 3766
maximum volume
112 μL
size
384 wells
working volume
80 μL
color
black
suitability
suitable for (cell cuture)
binding type
NBS™ (non-binding surface)
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Application
Corning® 384 well microplate, low flange has been used in enzyme activity assays to perform the phosphatase reactions. It has also been used to perform malachite green ATPase assays.
Features and Benefits
- Black wall plates provide low background fluorescence, minimal light scatter, and reduced crosstalk, ensuring accurate and precise measurements
- Thermally stable microplates (4°C to 37°C) ensure consistent performance over a wide range of temperature and storage conditions.
- Chemically stable and noncytotoxic microplates are designed to be compatible with aqueous solutions containing low levels (<20%) of organic solvents, including ethanol and DMSO.
- Meets SBS microplate standards to ensure compatibility with automated instruments.
- Suitable for bar coding
General description
Corning® 384-well ELISA Microplates with flat-bottom and low flange are high-quality, high-performance microplates that are widely used for laboratory assays. It improves assay sensitivity and performance.
Legal Information
Corning is a registered trademark of Corning, Inc.
NBS is a trademark of Corning, Inc.
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Nucleic acids research, 51(15), 8115-8132 (2023-07-03)
CRISPR-associated DinG protein (CasDinG) is essential to type IV-A CRISPR function. Here, we demonstrate that CasDinG from Pseudomonas aeruginosa strain 83 is an ATP-dependent 5'-3' DNA translocase that unwinds double-stranded (ds)DNA and RNA/DNA hybrids. The crystal structure of CasDinG reveals a
Markus Tiemann et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 28(57), e202201282-e202201282 (2022-07-06)
Discovery of protein-binding fragments for precisely defined binding sites is an unmet challenge to date. Herein, formylglycine is investigated as a molecular probe for the sensitive detection of fragments binding to a spatially defined protein site . Formylglycine peptide 3
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