L2164
Anti-Luciferase antibody, Mouse monoclonal
clone LUC-1, purified from hybridoma cell culture
Synonym(s):
Anti-Luciferase Antibody
Sign Into View Organizational & Contract Pricing
All Photos(3)
About This Item
Recommended Products
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
LUC-1, monoclonal
form
buffered aqueous solution
mol wt
60 kDa
enhanced validation
recombinant expression
Learn more about Antibody Enhanced Validation
concentration
~2 mg/mL
technique(s)
immunocytochemistry: 20-40 μg/mL using transfected 293Tcells expressing luciferase
immunocytochemistry: suitable
western blot: 2-4 μg/mL using whole extract of transfected 293T cells expressing luciferase
western blot: suitable
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Related Categories
General description
Anti-Luciferase antibody, Mouse monoclonal , (mouse IgG1 isotype) is derived from the LUC-1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with firefly (Photinus pyralis) luciferase. Luciferase, a reporter protein contains two binding pockets, one pocket for ATP and other one for luciferin substrate. Both the pockets are in close proximity to each other.
The mouse monoclonal Anti-Luciferase antibody recognizes the recombinant luciferase in transfected cells. This antibody provides user with an alternative detection method for luciferase. Since it directly detects the luciferase protein, it is not dependent on either the luciferase activity or the measeurement of rapid reaction kinetics. This also allows for the detection of the luciferase enzyme expression in situ with reproducibility between sample sets.
Specificity
Anti-Luciferase antibody, Mouse monoclonal recognizes recombinant luciferase in transfected eukaryotic (293T) cells.
Application
Anti-Luciferase antibody, Mouse monoclonal has been used in:
- immunoblotting
- immunocytochemistry
- immunohistochemistry
Biochem/physiol Actions
Luciferase catalyzes a bioluminescent reaction in the presence of substrate luciferin as well as Mg2+, oxygen and ATP. The luciferase assay is rapid, sensitive, and unlike the CAT assay, does not require a radioactive substrate. Anti-Luciferase antibody can detect the luciferase enzyme expression in situ, providing a means to study the cellular localization of the signal sequence activation.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
Working Dilution: 1-2 μg/ml
Storage and Stability
For continuous use store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in a frost-free freezer, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog, 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.
Not finding the right product?
Try our Product Selector Tool.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Jason R Becker et al.
Cardiovascular research, 93(3), 463-470 (2011-12-27)
Despite increased understanding of the fundamental biology regulating cardiomyocyte hypertrophy and heart failure, it has been challenging to find novel chemical or genetic modifiers of these pathways. Traditional cell-based methods do not model the complexity of an intact cardiovascular system
Calvin A Henard et al.
PLoS neglected tropical diseases, 8(7), e3000-e3000 (2014-07-18)
Professional phagocytes generate a myriad of antimicrobial molecules to kill invading microorganisms, of which nitrogen oxides are integral in controlling the obligate intracellular pathogen Leishmania. Although reactive nitrogen species produced by the inducible nitric oxide synthase (iNOS) can promote the
Sung-Yong Kim et al.
Plant physiology, 142(3), 984-992 (2006-09-12)
Extracellular ATP (eATP) in animals is well documented and known to play an important role in cellular signaling (e.g. at the nerve synapse). The existence of eATP has been postulated in plants; however, there is no definitive experimental evidence for
Dun Jack Fu et al.
Translational vision science & technology, 9(13), 44-44 (2021-01-15)
The purpose of this study was to develop and characterize a novel bioluminescence transgenic mouse model that facilitates rapid evaluation of genetic medicine delivery methods for inherited and acquired corneal diseases. Corneal expression of the firefly luciferase transgene (luc2) was
Mingxin Piao et al.
International journal of molecular sciences, 22(16) (2021-08-28)
Phytochromobilin (PΦB) participates in the regulation of plant growth and development as an important synthetase of photoreceptor phytochromes (phy). In addition, Arabidopsis long hypocotyl 2 (HY2) appropriately works as a key PΦB synthetase. However, whether HY2 takes part in the
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service