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SAB4200071

Sigma-Aldrich

ANTI-FLAG® antibody, Rat monoclonal

clone 6F7, purified from hybridoma cell culture

Synonyme(s) :

Anti-ddddk, Anti-dykddddk

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About This Item

Numéro MDL:
MFCD02262912
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.32

Source biologique

rat

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture
purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

6F7, monoclonal

Forme

buffered aqueous solution

Espèces réactives

all

Technique(s)

immunoprecipitation (IP): 2.5-5.0 μg using lysates of transiently transfected cells expressing C-terminal-FLAG-tagged protein
western blot: 0.5-1.0 μg/mL using extracts of transiently transfected cells expressing C-terminal-FLAG-tagged protein

Isotype

IgG1

Séquence immunogène

(DYKDDDDK)

Conditions d'expédition

dry ice

Température de stockage

−20°C

Description générale

Monoclonal Anti-FLAG® (rat IgG1 isotype) is derived from the hybridoma 6F7 produced by the fusion of mouse myeloma cells and splenocytes from rat immunized with the FLAG® peptide. The antibody is purified from culture supernatant of hybridoma cells grown in a bioreactor.

Monoclonal Anti-FLAG® recognizes N-terminal,
C-terminal and internal Flag-tagged fusion proteins. The product is especially recommended for identifying C-terminal FLAG®-tagged fusion proteins.
Epitope tags provide a method to localize gene products in a variety of cell types, study the topology of proteins and protein complexes, identify associated proteins, and characterize newly identified, low abundance, or poorly immunogenic proteins when protein specific antibodies are not available. Tagging with the FLAG® peptide sequence may be done at the N-terminus, N-terminus preceded by a methionine residue, C-terminus, or at internal positions of the target protein. FLAG may also be placed in associationith other tags. The small size of the FLAG® tag or sequence and its high hydrophilicity tend to decrease the possibility of interference with the protein expression, proteolytic maturation, antigenicity, and function.

The N-terminal FLAG® peptide sequence contains a unique enterokinase cleavage site allowing it to be completely removed from the purified fusion proteins. Cleavage of the C-terminal FLAG® peptide from a fusion protein catalyzed by Cu2+ ions has been reported. A sequence motif with five out of eight amino acid residues identical to the FLAG peptide is found in both rat and mouse Mg2+dependent protein b-phosphatase, as well as in the human and bovine enzyme.

Immunogène

FLAG peptide

DYKDDDDK

Application

ANTI-FLAG® antibody, Rat monoclonal has been used in:
  • chromatin immunoprecipitation (ChIP)
  • western blotting
  • coimmunoprecipitation
  • flow cytometric analysis

Learn more product details in our FLAG® application portal.
Browse additional application references in our FLAG® Literature portal.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Informations légales

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

PHF21B overexpression promotes cancer stem cell-like traits in prostate cancer cells by activating the Wntbeta-catenin signaling pathway
Li Q, et al
Journal of Experimental & Clinical Cancer Research, 36(1), 85-85 (2017)
Upregulated expression of HOXB7 in intrahepatic cholangiocarcinoma is associated with tumor cell metastasis and poor prognosis
Dai L, et al.
Laboratory Investigation; a Journal of Technical Methods and Pathology, 99(6), 736-736 (2019)
Xiaolei Li et al.
eLife, 6 (2017-08-19)
Acquired therapeutic resistance by tumors is a substantial impediment to reducing the morbidity and mortality that are attributable to human malignancies. The mechanisms responsible for the dramatic shift between chemosensitivity and chemoresistance in colorectal carcinoma have not been defined. Here
Rahul Bhowmick et al.
The Journal of biological chemistry, 287(42), 35004-35020 (2012-08-14)
Viruses have evolved to encode multifunctional proteins to control the intricate cellular signaling pathways by using very few viral proteins. Rotavirus is known to express six nonstructural and six structural proteins. Among them, NSP4 is the enterotoxin, known to disrupt
Qing Deng et al.
Cell death & disease, 9(11), 1049-1049 (2018-10-17)
PHD finger protein 19 (PHF19), a critical component of the polycomb repressive complex 2 (PRC2), is crucial for maintaining the repressive transcriptional activity of several developmental regulatory genes and plays essential roles in various biological processes. Abnormal expression of PHF19
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