F9291
ANTI-FLAG® BioM2 antibody, Mouse monoclonal
clone M2, purified immunoglobulin, buffered aqueous glycerol solution
동의어(들):
Monoclonal ANTI-FLAG® M2, Anti-ddddk, Anti-dykddddk
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
biotin conjugate
Clone:
M2, monoclonal
Application:
DB
Citations:
91
isotype
IgG1
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)
immunogen sequence
DYKDDDDK
shipped in
dry ice
storage temp.
−20°C
Quality Level
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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저장 등급
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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
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
Helen Hwang et al.
Scientific reports, 4, 6391-6391 (2014-09-30)
The ends of eukaryotic chromosomes are capped by telomeres which consist of tandem G-rich DNA repeats stabilized by the shelterin protein complex. Telomeres shorten progressively in most normal cells due to the end replication problem. In more than 85% of
Qing Xu et al.
Nature communications, 8(1), 425-425 (2017-09-06)
Tumor necrosis factor (TNF) has a critical role in diverse cellular events including inflammation, apoptosis and necroptosis through different signaling complexes. However, little is known about how the transition from inflammatory signaling to the engagement of death pathways is modulated.
Kenichiro Kawai et al.
PloS one, 6(11), e27106-e27106 (2011-11-11)
Nanoparticles (NPs) are small entities that consist of a hydroxyapatite core, which can bind ions, proteins, and other organic molecules from the surrounding environment. These small conglomerations can influence environmental calcium levels and have the potential to modulate calcium homeostasis
문서
Glycans play a key role in protein structure and disease; representation on cell surfaces is the glycome.
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