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Merck
모든 사진(1)

Key Documents

16-156

Millipore

Protein A Agarose, Fast Flow

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

동의어(들):

Protein A resin

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About This Item

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

형태

liquid

제조업체/상표

Upstate®

기술

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

배송 상태

wet ice

일반 설명

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

애플리케이션

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

품질

routinely evaluated in immunoprecipitation

물리적 형태

sterile distilled water containing 0.01% thimerosal

법적 정보

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1


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Ghia M Euskirchen et al.
Genome research, 17(6), 898-909 (2007-06-15)
Recent progress in mapping transcription factor (TF) binding regions can largely be credited to chromatin immunoprecipitation (ChIP) technologies. We compared strategies for mapping TF binding regions in mammalian cells using two different ChIP schemes: ChIP with DNA microarray analysis (ChIP-chip)
Lei Jiang et al.
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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

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