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SAB4200071

Sigma-Aldrich

ANTI-FLAG® antibody, Rat monoclonal

clone 6F7, purified from hybridoma cell culture

Sinônimo(s):

Anti-ddddk, Anti-dykddddk

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200 μL
R$ 2.842,00

R$ 2.842,00


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200 μL
R$ 2.842,00

About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.32

R$ 2.842,00


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fonte biológica

rat

conjugado

unconjugated

forma do anticorpo

purified from hybridoma cell culture
purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

6F7, monoclonal

Formulário

buffered aqueous solution

reatividade de espécies

all

técnica(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

Isotipo

IgG1

sequência de imunogênio

(DYKDDDDK)

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

Descrição geral

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.[1] 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.[2] 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[3], as well as in the human and bovine enzyme.

Imunogênio

FLAG peptide

DYKDDDDK

Aplicação

ANTI-FLAG® antibody, Rat monoclonal has been used in:
  • chromatin immunoprecipitation (ChIP)[4]
  • western blotting[5]
  • coimmunoprecipitation[6][7]
  • flow cytometric analysis[7]

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

forma física

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

Informações legais

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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Código de classe de armazenamento

10 - Combustible liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


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Visite a Biblioteca de Documentos

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)
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
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
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)
Rotaviral enterotoxin nonstructural protein 4 targets mitochondria for activation of apoptosis during infection
Bhowmick R, et al.
The Journal of Biological Chemistry, 287(42), 35004-35020 (2012)

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