F2922
Monoclonal Anti-FLAG® BioM5−Biotin antibody produced in mouse
clone M5, purified immunoglobulin, buffered aqueous solution
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About This Item
MDL number:
UNSPSC Code:
12352203
Recommended Products
biological source
mouse
conjugate
biotin conjugate
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
M5, monoclonal
form
buffered aqueous solution
technique(s)
western blot (chemiluminescent): 2 μg/mL
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
General description
Anti-FLAG® BioM5 monoclonal antibody is a purified murine IgG1 monoclonal antibody that is covalently attached by hydrazide linkage. It can be detected by avidin or streptadivin conjugates.
Application
Anti-FLAG® BioM5 monoclonal antibody is useful for Western blotting, microscopy applications and formation of avidin-biotin complexes (ABC) in mammalian and Drosophila cells. Anti-FLAG® BioM5 antibody in combination with an avidin or streptavidin conjugate is the preferred anti-FLAG® antibody for detection of FLAG fusion proteins expressed in mouse cells.
The product binds the FLAG peptide only when it is located at the amino terminus preceded by a methionine. Binding is not Ca2+-dependent. It is useful for detecting cytoplasmically expressed Met-FLAG® fusion proteins in mammalian crude cell extracts, but not recommended for fusion proteins expressed in E. coli.
It can be 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.
Browse additional application references in our FLAG® Literature portal.
The product binds the FLAG peptide only when it is located at the amino terminus preceded by a methionine. Binding is not Ca2+-dependent. It is useful for detecting cytoplasmically expressed Met-FLAG® fusion proteins in mammalian crude cell extracts, but not recommended for fusion proteins expressed in E. coli.
It can be 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.
Browse additional application references in our FLAG® Literature portal.
Binds the FLAG peptide only when it is located at the amino terminus preceded by a methionine. Binding is not Ca2+-dependent. Useful for detecting cytoplasmically expressed Met-FLAG fusion proteins in mammalian crude cell extracts, but not recommended for fusion proteins expressed in E. coli.
Features and Benefits
ANTI-FLAG M5 − Biotin conjugate has a high affinity for N-terminal Met-FLAG fusion proteins.
Physical form
Solution in 10 mM sodium phosphate, pH 7.4, containing 150 mM NaCl and 0.02% sodium azide
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
12 - Non Combustible Liquids
wgk_germany
WGK 3
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’.
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Xinna Zhang et al.
The EMBO journal, 30(11), 2177-2189 (2011-04-28)
Tumour suppressor p53 levels in the cell are tightly regulated by controlled degradation through ubiquitin ligases including Mdm2, COP1, Pirh2, and ARF-BP1. The ubiquitination process is reversible via deubiquitinating enzymes, such as ubiquitin-specific peptidases (USPs). In this study, we identified
Jin-Ho Koh et al.
Cell metabolism, 25(5), 1176-1185 (2017-05-04)
The objective of this study was to evaluate the specific mechanism(s) by which PPARβ regulates mitochondrial content in skeletal muscle. We discovered that PPARβ increases PGC-1α by protecting it from degradation by binding to PGC-1α and limiting ubiquitination. PPARβ also
Peipei Wang et al.
The Journal of biological chemistry, 299(8), 105055-105055 (2023-07-17)
Post-translational modifications including protein ubiquitination regulate a plethora of cellular processes in distinct manners. RNA N6-methyladenosine is the most abundant post-transcriptional modification on mammalian mRNAs and plays important roles in various physiological and pathological conditions including hematologic malignancies. We previously
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