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About This Item
NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
biotin conjugate
Clone:
M2, monoclonal
Application:
DB
Citations:
128
Quality Level
biological source
mouse
conjugate
biotin conjugate
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
M2, monoclonal
form
buffered aqueous glycerol solution
species reactivity
all
concentration
~1 mg/mL
technique(s)
dot blot: suitable (chemiluminescent detection)
isotype
IgG1
immunogen sequence
DYKDDDDK
shipped in
dry ice
storage temp.
−20°C
General description
The monoclonal Anti-FLAG BioM2 mouse antibody is covalently attached to biotin by hydrazide linkage. The antibody recognizes the FLAG sequence at the N-terminus, Met-N-terminus or C-terminus of FLAG fusion porteins.
Application
Biotin-labeled antibody is used for immunodetection methods using avidin- or streptavidin-conjugated reporter enzymes such as streptavidin-peroxidase. Primary antibody conjugates are preferred when using murine cells as the recombinant protein host.
Antibody is suitable for immunofluorescence, western blotting, microscopy applications and for the formation of avidin-biotin complexes.
Learn more product details in our FLAG® application portal.
Antibody is suitable for immunofluorescence, western blotting, microscopy applications and for the formation of avidin-biotin complexes.
Learn more product details in our FLAG® application portal.
Physical form
Solution in 50% glycerol, 10 mM sodium phosphate, pH 7.25, containing 150 mM NaCl and 0.02% sodium azide
Preparation Note
Dilute antibody in TBS (.05M Tris, pH7.4, with .15M NaCl) to a final concentration of 1-10μg/mL.
Legal Information
ANTI-FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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Nawal Bendris et al.
PloS one, 6(7), e22879-e22879 (2011-08-11)
Cyclin A2 is essential at two critical points in the somatic cell cycle: during S phase, when it activates CDK2, and during the G2 to M transition when it activates CDK1. Based on the crystal structure of Cyclin A2 in
Yoori Kim et al.
Scientific reports, 7(1), 2071-2071 (2017-05-20)
Single-molecule studies of protein-nucleic acid interactions frequently require site-specific modification of long DNA substrates. The bacteriophage λ is a convenient source of high quality long (48.5 kb) DNA. However, introducing specific sequences, tertiary structures, and chemical modifications into λ-DNA remains technically
Hong-Won Lee et al.
Nature communications, 4, 1505-1505 (2013-02-21)
Co-immunoprecipitation (co-IP) has become a standard technique, but its protein-band output provides only static, qualitative information about protein-protein interactions. Here we demonstrate a real-time single-molecule co-IP technique that generates real-time videos of individual protein-protein interactions as they occur in unpurified