F2922
Monoclonal Anti-FLAG® BioM5−Biotin antibody produced in mouse
clone M5, purified immunoglobulin, buffered aqueous solution
Sign Into View Organizational & Contract Pricing
All Photos(1)
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
Not finding the right product?
Try our Product Selector Tool.
Storage Class Code
12 - Non Combustible Liquids
WGK
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
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