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Thermo Scientific™ Pierce™ p-Aminophenyl Phosphoryl Choline Agarose

Bind and purify C-reactive protein (CRP) using these agarose beads of immobilized p-aminophenyl phosphoryl choline (APC).

Supplier:  Thermo Scientific™ 20307

Catalog No. PI20307


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Description

Description

Thermo Scientific™ Pierce p-Amino Phosphoryl Choline Agarose enables the purification of C-reactive protein (CRP).

Immobilized phosphoryl choline is a beaded agarose affinity resin for purification of C-reactive protein (CRP) from plasma, ascites and other biological fluids. CRP is a pentameric (pentraxin) protein that is classified as an acute phase reactant because of its high level of production during inflammation. The protein binds to phosphoryl choline groups on the surface of microbes and has been linked to several biological functions including activation of the classical complement pathway, enhancement of phagocytosis and interaction with certain subpopulations of T-lymphocytes. In the late 1970s, Volanakis and colleagues discovered a method of isolating and studying C-reactive protein by using the protein's affinity for phosphoryl choline that has been immobilized to a porous solid chromatography support.

Highlights:

  • Ligand – p-aminophenyl phosphoryl choline

  • Support – crosslinked 6% beaded agarose

  • Binding capacity – greater than 3mg of human C-reactive protein per milliliter of settled resin

  • Format – 50% resin slurry in 0.02% sodium azide

  • Binding Condition – Tris or borate-buffered saline (pH 8 to 8.5) with 1 to 2mM calcium chloride

  • Elution Condition – Tris or borate-buffered saline (pH 8 to 8.5) with 2mM EDTA

  • Reusable – resin can be regenerated and reused several times

Recommended for:

Purify c-reactive protein (CRP); Purify anti-p-Aminophenyl phosphoryl choline antibodies

Specifications

Specifications

Upon receipt store at 4°C.
Pierce™
C-reactive Protein
p-Amino Phosphoryl Choline
Affinity, Agarose Resin
Liquid
5 mL
Agarose
Bottle
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For Research Use Only. Not for use in diagnostic procedures.