Heparin sepharose hp column

Manufactured by GE Healthcare

Sourced in United States

The Heparin–sepharose HP column is a chromatography column used for the purification and separation of various biomolecules, including enzymes, growth factors, and coagulation factors. It utilizes the affinity of heparin, a naturally occurring anticoagulant, to bind and retain specific target proteins, allowing for their isolation and concentration from complex mixtures.

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Lab products found in correlation

Nickel column, by Qiagen (1 mentions) Nickel resin, by Qiagen (1 mentions)

Close spelling variants of this product

Heparin column (44 citations) Heparin Sepharose (27 citations) Heparin-Sepharose column (24 citations) Heparin HP column (10 citations) Heparin (8 citations)

2 protocols using heparin sepharose hp column

Purification and Characterization of HCV Proteins

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NS3-FL pellets were resuspended, lysed, loaded onto a nickel column
(Qiagen), washed, and eluted. Gradient peaks were collected, dialyzed,
centrifuged, and loaded on a heparin–sepharose HP column (GE).
Peak fractions were pooled and stored at −80 °C. NS3 protease,
NS3 helicase, NS5A-Δ32, pellets were handled as described above,
except that a Superdex 75 column was used instead of heparin–sepharose
HP. NS5B-Δ21 was purified using the following three successive
columns: nickel, SP Sepharose, and Superdex 200. NS5B-FL was batch-purified
using nickel resin (Qiagen). See Supporting Information for additional details.

Cho N.J., Pham E.A., Hagey R.J., Lévêque V.J., Ma H., Klumpp K, & Glenn J.S. (2016). Reconstitution and Functional Analysis of a Full-Length Hepatitis C Virus NS5B Polymerase on a Supported Lipid Bilayer. ACS Central Science, 2(7), 456-466.

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Purification and Characterization of Rennet

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(NH₄)₂SO₄ (40 g per 100 mL) was added to the c.f. containing active rChn-Alc-KL, stirred for 30 min, and left at 4 °C for 20 h. Then the precipitate was separated by centrifugation (13,130× g, 4 °C, 40 min), dissolved in buffer A (50 mM Na-acetate buffer, pH 5.0, 2.0 M NaCl), and applied to a Phenyl Seplife HP column (“Sunresin”, Shaanxi, China). The column was washed with the buffer until the release of proteins that did not bind to the hydrophobic sorbent. Fractions containing rChn-Alc-KL were eluted with buffer B (50 mM Na-acetate buffer, pH 5.0), combined, and applied to a Heparin Sepharose HP column (“GE Healthcare”, Salt Lake, UT, USA). The column was washed with buffer B until the removal of the material that did not bind to the carrier. The target enzyme was eluted with buffer B containing 0.25 M NaCl.
Total milk-clotting activity, total proteolytic activity, thermal stability, and dependence of the coagulation time on CaCl₂ concentration and pH were determined according to [21 (link)].

Balabova D.V., Belash E.A., Belenkaya S.V., Shcherbakov D.N., Belov A.N., Koval A.D., Mironova A.V., Bondar A.A., Volosnikova E.A., Arkhipov S.G., Sokolova O.O., Chirkova V.Y, & Elchaninov V.V. (2023). Biochemical Properties of a Promising Milk-Clotting Enzyme, Moose (Alces alces) Recombinant Chymosin. Foods, 12(20), 3772.

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