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F2922

Sigma-Aldrich

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:
MFCD01633351
UNSPSC Code:
12352203

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.
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 Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

F2922-.2MG:
F2922-1MG:
F2922-BULK:
F2922-VAR:

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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