F3165

Sigma-Aldrich

Monoclonal ANTI-FLAG® M2 antibody produced in mouse

clone M2, purified immunoglobulin (Purified IgG1 subclass), buffered aqueous solution (10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide)

Synonym(s):
Anti-ddddk, Anti-dykddddk
NACRES:
NA.32

Quality Level

biological source

mouse

antibody form

purified immunoglobulin (Purified IgG1 subclass)

antibody product type

primary antibodies

clone

M2, monoclonal

form

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

purified by

using Protein A

species reactivity

all

concentration

3.8-4.2 mg/mL

application(s)

western blot: 10 μg/mL (Protein A)

isotype

IgG1

immunogen sequence

DYKDDDDK

conjugate

unconjugated

shipped in

dry ice

storage temp.

−20°C

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General description

Anti Flag M2 antibody is used for the detection of Flag fusion proteins.This monoclonal antibody is produced in mouse and recognizes the FLAG sequence at the N-terminus, Met N-terminus, and C-terminus. The antibody is also able to recognize FLAG at an internal site. M2, unlike M1 antibody is not Calcium dependent.
F1804 is an affinity purified, FLAG M2 antibody, increasing sensitivity in most applications.
Method of purification - Protein A

Immunogen

FLAG; peptide sequence DYKDDDDK

Application

Monoclonal ANTI-FLAG® M2 antibody produced in mouse has been used in:
  • immunoblotting
  • immunoprecipitation
  • immunocytochemistry
  • immunofluorescence
  • ELISA
  • EIA
  • chromatin immunoprecipitation
  • electron microscopy
  • flow cytometry
  • supershift assays

Browse additional application references in our FLAG® Literature portal.

Packaging

5 mg in poly bottle

Preparation Note

Dilute the antibody solution from 0.5-10 ug/mL in Tris Buffered Saline, pH 8.0, with 3% nonfat milk

Storage and Stability

Store the undiluted antibody at –20 °C in working aliquots. Repeated freezing and thawing is not recommended.
Note: Overtime, small amounts of purified antibodies can precipitate from solution due to intermolecular hydrophobic interactions. If a precipitate is observed in this product, briefly centrifuge the vial to pellet the precipitate. Withdraw the desired volume of antibody solution from the clear supernatant for use. This should not alter the performance of the purified antibody in Western blot or immunoprecipitation applications.

Legal Information

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

storage_class_code

12 - Non Combustible Liquids

WGK Germany

nwg

Flash Point F

Not applicable

Flash Point C

Not applicable

Certificate of Analysis

Certificate of Origin

Casey C Fowler et al.
Nature communications, 10(1), 3684-3684 (2019-08-17)
Bacterial toxins with an AB5 architecture consist of an active (A) subunit inserted into a ring-like platform comprised of five delivery (B) subunits. Salmonella Typhi, the cause of typhoid fever, produces an unusual A2B5 toxin known as typhoid toxin. Here...
Fangzhi Tan et al.
Nature communications, 10(1), 3733-3733 (2019-08-21)
Hearing loss is the most common sensory disorder. While gene therapy has emerged as a promising treatment of inherited diseases like hearing loss, it is dependent on the identification of gene delivery vectors. Adeno-associated virus (AAV) vector-mediated gene therapy has...
Hong Zhu et al.
Molecular biology of the cell, 24(11), 1619-1637 (2013-04-12)
Charcot-Marie-Tooth (CMT) disease is an inherited neurological disorder. Mutations in the small integral membrane protein of the lysosome/late endosome (SIMPLE) account for the rare autosomal-dominant demyelination in CMT1C patients. Understanding the molecular basis of CMT1C pathogenesis is impeded, in part...
Jeong Gu Kang et al.
Scientific reports, 9(1), 11960-11960 (2019-08-21)
Despite the increased interest in epigenetic research, its progress has been hampered by a lack of satisfactory tools to control epigenetic factors in specific genomic regions. Until now, many attempts to manipulate DNA methylation have been made using drugs but...
Annie M Sriramachandran et al.
Nature communications, 10(1), 3678-3678 (2019-08-17)
Modification with SUMO regulates many eukaryotic proteins. Down-regulation of sumoylated forms of proteins involves either their desumoylation, and hence recycling of the unmodified form, or their proteolytic targeting by ubiquitin ligases that recognize their SUMO modification (termed STUbL or ULS)....
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