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Merck

16-156

Protein A Agarose, Fast Flow

Protein A Agarose, Fast Flow suitable for medium and low-pressure chromatography, immunoprecipitation and antibody purification.

Synonym(s):

Protein A resin

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About This Item

UNSPSC Code:
41116133
NACRES:
NA.56
eCl@ss:
32160801

Key Documents

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Product Name

Protein A Agarose, Fast Flow, Protein A Agarose, Fast Flow suitable for medium and low-pressure chromatography, immunoprecipitation and antibody purification.

form

liquid

manufacturer/tradename

Upstate®

technique(s)

affinity chromatography: suitable
immunoprecipitation (IP): suitable
western blot: suitable

shipped in

wet ice

Analysis Note

routinely evaluated in immunoprecipitation

Application

Protein A Agarose, Fast Flow has been used in immunoprecipitation and chromatin immunoprecipitation (ChIP).

Disclaimer

For U.S. Customers: Contains mercury; Do not place in trash - dispose according to local, state, or federal laws.

General description

Protein A is an immunoglobulin (Ig)-binding protein used to purify large amounts of IgG. It binds to the Fc part of the antibody at the CH2–CH3 interface. Protein A-agarose might be suitable for low-pressure antibody isolation.
Recombinant Protein A covalently coupled to highly cross-linked 6% agarose beads.

Binding capacity: 40mg human IgG/ml agarose

Physical form

sterile distilled water containing 0.01% thimerosal

Legal Information

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

Storage Class

10 - Combustible liquids

wgk

WGK 1

Certificates of Analysis (COA)

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Yong Cheng et al.
Nature, 515(7527), 371-375 (2014-11-21)
To broaden our understanding of the evolution of gene regulation mechanisms, we generated occupancy profiles for 34 orthologous transcription factors (TFs) in human-mouse erythroid progenitor, lymphoblast and embryonic stem-cell lines. By combining the genome-wide transcription factor occupancy repertoires, associated epigenetic
Vasavi Sundaram et al.
Genome research, 24(12), 1963-1976 (2014-10-17)
Transposable elements (TEs) have been shown to contain functional binding sites for certain transcription factors (TFs). However, the extent to which TEs contribute to the evolution of TF binding sites is not well known. We comprehensively mapped binding sites for
Suzana Markolovic et al.
Nature chemical biology, 14(7), 688-695 (2018-06-20)
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical
Lei Jiang et al.
Investigative ophthalmology & visual science, 61(5), 41-41 (2020-05-24)
To identify the pathogenic gene of infantile nystagmus syndrome (INS) in three Chinese families and explore the potential pathogenic mechanism of FERM domain-containing 7 (FRMD7) mutations. Genetic testing was performed via Sanger sequencing. Western blotting was used to analyze protein
Simon Schenk et al.
American journal of physiology. Endocrinology and metabolism, 291(2), E254-E260 (2006-05-04)
Although the increase in fatty acid oxidation after endurance exercise training has been linked with improvements in insulin sensitivity and overall metabolic health, the mechanisms responsible for increasing fatty acid oxidation after exercise training are not completely understood. The primary
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