产品名称
Anti-Renilla Luciferase Antibody, clone 1D5.2, ascites fluid, clone 1D5.2, Chemicon®
biological source
mouse
antibody form
ascites fluid
antibody product type
primary antibodies
clone
1D5.2, monoclonal
species reactivity (predicted by homology)
all
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
western blot: suitable
isotype
IgG
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Physical form
Liquid.
Unpurified
Analysis Note
Control
Renilla
Renilla
Application
Immunoblotting
EIA
Optimal working dilutions must be determined by end user.
EIA
Optimal working dilutions must be determined by end user.
Research Category
Epitope Tags & General Use
Epitope Tags & General Use
Research Sub Category
Epitope Tags
Epitope Tags
This Anti-Renilla Luciferase Antibody, clone 1D5.2 is validated for use in ELISA, WB for the detection of Renilla Luciferase.
Biochem/physiol Actions
Recognizes Renilla luciferase.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
36 kDa
Immunogen
Renilla luciferase GST fusion protein.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Preparation Note
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Ruth Röck et al.
Scientific reports, 5, 11133-11133 (2015-06-24)
Membrane receptor-sensed input signals affect and modulate intracellular protein-protein interactions (PPIs). Consequent changes occur to the compositions of protein complexes, protein localization and intermolecular binding affinities. Alterations of compartmentalized PPIs emanating from certain deregulated kinases are implicated in the manifestation
Johanna E Mayrhofer et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(49), 31105-31113 (2020-11-25)
Kinase-targeted therapies have the potential to improve the survival of patients with cancer. However, the cancer-specific spectrum of kinase alterations exhibits distinct functional properties and requires mutation-oriented drug treatments. Besides post-translational modifications and diverse intermolecular interactions of kinases, it is
Hans H Schiffer et al.
Molecular pharmacology, 71(2), 508-518 (2006-09-14)
We have developed a new assay for measuring epidermal growth factor receptor (EGFR) activation using the bioluminescence resonance energy transfer (BRET) technology, which directly measures the recruitment of signaling proteins to activated EGFR. Our results demonstrate that EGFR BRET assays
Graham J Belsham et al.
RNA (New York, N.Y.), 14(8), 1671-1680 (2008-06-24)
The initiation of protein synthesis on mRNAs within eukaryotic cells is achieved either by a 5' cap-dependent mechanism or through internal initiation directed by an internal ribosome entry site (IRES). Picornavirus IRES elements, located in the 5' untranslated region (5'UTR)
Mickaël Bouvet et al.
The Journal of biological chemistry, 289(37), 25783-25796 (2014-07-31)
The RNA-synthesizing machinery of the severe acute respiratory syndrome Coronavirus (SARS-CoV) is composed of 16 non-structural proteins (nsp1-16) encoded by ORF1a/1b. The 148-amino acid nsp10 subunit contains two zinc fingers and is known to interact with both nsp14 and nsp16
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