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P9424

Millipore

Proteína A – Agarosa

aqueous ethanol suspension

Sinónimos:

Protein A–Agarose

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About This Item

MDL number:
MFCD00165563
UNSPSC Code:
41106500
NACRES:
NA.56

biological source

Staphylococcus aureus

form

aqueous ethanol suspension

analyte chemical class(es)

proteins (Immunoglobulins of various mammalian species)

extent of labeling

~6 mg per mL

technique(s)

affinity chromatography: suitable

matrix

Sepharose 4B Fast Flow

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

capacity

≥30 mg/mL binding capacity (human IgG)

storage temp.

2-8°C

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General description

Protein A-Sepharose™ has been used to develop strategies for investigating protein interactions, to improve the detection of celiac disease, and to study diabetes in children.

Application

Protein A-Sepharose is used for affinity chromatography, antibody purification and characterization, immunoaffinity matrices, protein chromatography, protein A, G and L resins, and recombinant protein expression and analysis. Protein A-Sepharose™ has been used to develop strategies for investigating protein interactions, to improve the detection of celiac disease, and to study diabetes in children.
Protein A-Sepharose™ Fast Flow from Staphylococcus aureus has been used:
  • in co-immunoprecipitation assay
  • in immunodepletion
  • to purify IgG from human serum and plasma

Physical form

Suspension in 20% ethanol

Legal Information

Sepharose is a trademark of Cytiva

pictograms

Flame
GHS02

signalword

Warning

hcodes

H226

Hazard Classifications

Flam. Liq. 3

wgk_germany

WGK 3

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Joyce A Benjamins et al.
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To identify whether factors toxic to oligodendrocytes (OLs), released by B cells from patients with MS, are found in extracellular microvesicles enriched in exosomes. Conditioned medium (Sup) was obtained from cultures of blood B cells of patients with MS and
H Sternlicht et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(20), 9422-9426 (1993-10-15)
A role in folding newly translated cytoskeletal proteins in the cytosol of eukaryotes has been proposed for t-complex polypeptide 1 (TCP1). In this study, we investigated tubulin and actin biogenesis in Chinese hamster ovary (CHO) cells. When extracts of pulse-labeled
C Macaulay et al.
The Journal of biological chemistry, 270(1), 254-262 (1995-01-06)
During each cell cycle, the nucleus of higher eukaryotes undergoes a dramatic assembly and disassembly. These events can be faithfully reproduced in vitro using cell-free extracts derived from Xenopus eggs. Such extracts contain three major N-acetylglucosaminylated proteins, p200, p97, and
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European journal of immunology, 41(5), 1288-1297 (2011-04-07)
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