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A9594

Sigma-Aldrich

Monoclonal ANTI-FLAG® M2-Cy3™ antibody produced in mouse

clone M2, purified immunoglobulin, buffered aqueous solution (Supplied as a solution in 10 mM sodium phosphate)

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Synonym(s):
Monoclonal ANTI-FLAG® M2 antibody produced in mouse, Anti-ddddk, Anti-dykddddk
NACRES:
NA.32

biological source

mouse

Quality Level

200

conjugate

CY3 conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

M2, monoclonal

form

buffered aqueous solution (Supplied as a solution in 10 mM sodium phosphate)

species reactivity

all

concentration

~1 mg/mL

technique(s)

direct immunofluorescence: 10 μg/mL using mammalian cells fixed with methanol:acetone

isotype

IgG1

immunogen sequence

DYKDDDDK

shipped in

dry ice

storage temp.

−20°C

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F4049F3165F1804
Monoclonal ANTI-FLAG® M2-Cy3™ antibody produced in mouse clone M2, purified immunoglobulin, buffered aqueous solution (Supplied as a solution in 10 mM sodium phosphate)

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A9594

Monoclonal ANTI-FLAG® M2-Cy3™ antibody produced in mouse

Monoclonal ANTI-FLAG® M2-FITC antibody produced in mouse clone M2, purified immunoglobulin, buffered aqueous solution

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F4049

Monoclonal ANTI-FLAG® M2-FITC antibody produced in mouse

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Sigma-Aldrich

F3165

Monoclonal ANTI-FLAG® M2 antibody produced in mouse

Monoclonal ANTI-FLAG® M2 antibody produced in mouse 1 mg/mL, clone M2, affinity isolated antibody, buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)

Sigma-Aldrich

F1804

Monoclonal ANTI-FLAG® M2 antibody produced in mouse

conjugate

CY3 conjugate

conjugate

FITC conjugate

conjugate

unconjugated

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin (Purified IgG1 subclass)

antibody form

affinity isolated antibody

clone

M2, monoclonal

clone

M2, monoclonal

clone

M2, monoclonal

clone

M2, monoclonal

form

buffered aqueous solution (Supplied as a solution in 10 mM sodium phosphate)

form

buffered aqueous solution

form

buffered aqueous solution (10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide)

form

buffered aqueous solution (50% glycerol, 10 mM sodium phosphate, and 150 mM NaCl, pH 7.4)

species reactivity

all

species reactivity

all

species reactivity

all

species reactivity

all

General description

Monoclonal ANTI-FLAG M2-Cy3 (mouse IgG) antibody is covalently conjugated to cyanine dye Cy3. The antibody conjugate binds to FLAG fusion proteins, and will recognize the FLAG sequence at the N-terminus, Met-N-terminus, or C-terminus of FLAG fusion proteins.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
For simple, one-step detection by immunocytochemistry. Especially useful in detection of FLAG fusion proteins expressed in murine host, where secondary anti-mouse antibodies might cause cross-reactivity.

Browse additional application references in our FLAG® Literature portal.

Physical form

Solution in phosphate buffered saline plus 1% BSA and preservative

Preparation Note

Dilute the antibody in Tris buffered saline (TBS): 0.05 M Tris,pH 7.4, with 0.15 M NaCl.

Other Notes

Suggested concentration of 1-10 mg/ml for immunocytochemistry.

Legal Information

ANTI-FLAG is a registered trademark of Sigma-Aldrich Co. LLC
Cy3 is a trademark of Cytiva
FLAG is a registered trademark of Sigma-Aldrich Co. LLC

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Takeshi Yoshizumi et al.
Biomacromolecules, 19(5), 1582-1591 (2018-03-31)
Selective gene delivery into organellar genomes (mitochondrial and plastid genomes) has been limited because of a lack of appropriate platform technology, even though these organelles are essential for metabolite and energy production. Techniques for selective organellar modification are needed to
Robert S Ohgami et al.
Blood, 108(4), 1388-1394 (2006-04-13)
Iron and copper are essential for all organisms, assuming critical roles as cofactors in many enzymes. In eukaryotes, the transmembrane transport of these elements is a highly regulated process facilitated by the single electron reduction of each metal. Previously, we
Oliver Wicht et al.
Journal of virology, 88(9), 4943-4952 (2014-02-21)
Enveloped viruses carry highly specialized glycoproteins that catalyze membrane fusion under strict spatial and temporal control. To prevent premature activation after biosynthesis, viral class I fusion proteins adopt a locked conformation and require proteolytic cleavage to render them fusion-ready. This
Saifeng Wang et al.
Genes & development, 33(15-16), 1048-1068 (2019-06-22)
Fetal hematopoietic stem and progenitor cells (HSPCs) hold promise to cure a wide array of hematological diseases, and we previously found a role for the RNA-binding protein (RBP) Lin28b in respecifying adult HSPCs to resemble their fetal counterparts. Here we
Joanna Lawrence et al.
Molecular pharmacology, 67(6), 1822-1828 (2005-03-22)
The small GTP-binding protein ADP ribosylation factor 6 (ARF6) has recently been implicated in the internalization of G protein-coupled receptors (GPCRs), although its precise molecular mechanism in this process remains unclear. We have recently identified centaurin alpha(1) as a GTPase
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