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Merck

SAB4200119

Monoclonal Anti-FLAG-Peroxidase antibody produced in rat

2-4 mg/mL, clone 6F7, purified immunoglobulin

Synonyme(s) :

Anti-ddddk, Anti-dykddddk

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A propos de cet article

NACRES:
NA.32
UNSPSC Code:
12352203
Conjugate:
peroxidase conjugate
Clone:
6F7, monoclonal
Application:
WB
Citations:
9
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biological source

rat

conjugate

peroxidase conjugate

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

6F7, monoclonal

form

buffered aqueous solution

species reactivity

all

concentration

2-4 mg/mL

technique(s)

western blot: 1:1,000-1:2,000 using extracts of transfected cells expressing C-terminal FLAG-tagged fusion protein

isotype

IgG1

immunogen sequence

DYKDDDDK

shipped in

dry ice

storage temp.

−20°C

Quality Level

General description

Monoclonal Anti-FLAG-Peroxidase is a purified immunoglobulin fraction of monoclonal Anti-FLAG (rat IgG1 isotype) isolated from culture supernatant of the 6F7 hybridoma cells grown in a bioreactor, conjugated to horseradish peroxidase (HRP). The hybridoma 6F7 was produced by the fusion of mouse myeloma cells and splenocytes from rat immunized with the FLAG peptide.
The product recognizes N-terminal, C-terminal, and internal FLAG-tagged fusion proteins. It is especially recommended for identifying C-terminal FLAG-tagged fusion proteins.

Immunogen

purified immunoglobulin fraction of monoclonal Anti-FLAG (rat IgG1 isotype) isolated from culture supernatant of the 6F7 hybridoma cells grown in a bioreactor, conjugated to horseradish peroxidase (HRP).

Application

Learn more product details in our FLAG® applications portal.
Monoclonal Anti-FLAG-Peroxidase, recognizes N-terminal, C-terminal and internal FLAG-tagged fusion proteins. The product is especially recommended for identifying C-terminal FLAG-tagged fusion proteins. The product can be used for immunoblotting.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.01% merthiolate.

Legal Information

FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

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Classe de stockage

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


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Consulter la Bibliothèque de documents

Jasjot Singh et al.
Nature communications, 13(1), 6212-6212 (2022-10-21)
Lysosomes are well-established as the main cellular organelles for the degradation of macromolecules and emerging as regulatory centers of metabolism. They are of crucial importance for cellular homeostasis, which is exemplified by a plethora of disorders related to alterations in
Meidi Gu et al.
Nature immunology, 22(2), 193-204 (2021-01-06)
Metabolic reprograming toward aerobic glycolysis is a pivotal mechanism shaping immune responses. Here we show that deficiency in NF-κB-inducing kinase (NIK) impairs glycolysis induction, rendering CD8+ effector T cells hypofunctional in the tumor microenvironment. Conversely, ectopic expression of NIK promotes
Claudia Isabelle Keller Valsecchi et al.
Nature, 589(7840), 137-142 (2020-11-20)
Confinement of the X chromosome to a territory for dosage compensation is a prime example of how subnuclear compartmentalization is used to regulate transcription at the megabase scale. In Drosophila melanogaster, two sex-specific non-coding RNAs (roX1 and roX2) are transcribed
Jente Stouthamer et al.
Methods in molecular biology (Clifton, N.J.), 2690, 193-204 (2023-07-14)
Interactions between extracellular domains (ECDs) are crucial for many physiological processes in the cell, most importantly perception of its environment. However, studying these often-transient interactions can be challenging. Here we describe a method that allows for in vitro detection of
DongHyuk Lee et al.
Nature communications, 11(1), 1838-1838 (2020-04-17)
Production of reactive oxygen species (ROS) is critical for successful activation of immune responses against pathogen infection. The plant NADPH oxidase RBOHD is a primary player in ROS production during innate immunity. However, how RBOHD is negatively regulated remains elusive.

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