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GE17371201

Ni Sepharose Excel, 25 ML

Cytiva 17371201, 90 μm avg. part. size

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Synonym(s):
Ni Sepharose Excel
UNSPSC Code:
41106500
NACRES:
NA.56

manufacturer/tradename

Cytiva 17371201

matrix

highly cross-linked 6% agarose

avg. part. size

90 μm

cleaning in place

2-14

working range

2-12

capacity

≥10 mg binding capacity (histidine-tagged protein)()Dynamic binding capacity was tested with 0.5 mg/ml (histidine)6-tagged pure protein (Mr 43 000) in EX-CELL 420 Insect serum-free medium (capacity at 10% breakthrough) or (histidine)6-tagged protein (Mr 28 000). Column volume was 1 ml and flow rate 1 ml/min. Binding capacity is sample-dependent.)

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General description

Ni Sepharose excel is a his-tagged protein purification resin for minimized Ni-leakage and maximized protein recovery when samples contain stripping agents.

EDTA-resistant resin for IMAC chromatography: Ni Sepharose excel is an IMAC resin precharged with nickel ions that are very strongly bound to a chelating ligand. Nickel ions remain bound to the ligand even after 24 h incubation in 10 mM EDTA. Because of this strong binding, samples that typically cause stripping of metal ions can be loaded directly onto the resin without time-consuming pretreatment. Therefore, this his tag purification resin is especially suitable for purifying histidine-tagged (his-tagged) proteins secreted into eukaryotic cell culture supernatants.

His tag purification of large sample volumes: The flow properties of Ni Sepharose excel nickel resin make it well-suited to purification at a wide range of scales. This resin can handle loading of large sample volumes, so you can purify low concentrations of target proteins using manual or automated methods.

Convenient prepacked columns:
  • HisTrap excel column: HiTrap format for convenient use with a syringe, a peristaltic pump, or a chromatography system.
  • His MagSepharose excel: Magnetic beads for small-scale purification and screening. They are appropriate for early stages of research when many parallel experiments are required.

Features and Benefits

  • Versatile – suitable for eukaryotic samples, including insect and CHO cells, as well as bacterial samples such as E. coli.
  • Direct sample load – of eukaryotic cell culture supernatants, eliminating the need for pretreatment of samples that usually cause nickel stripping.
  • Retained binding capacity of up to 10 mg/mL resin.
  • Simplified sample handling – fewer steps needed compared with conventional workflow.
  • Flexible formats – prepacked and loose resin formats for optimized screening and preparative his-tag purification.

Storage and Stability

Store at 4 to 30 °C (20% ethanol)

Analysis Note

To view the Certificate of Analysis for this product, please visit www.cytiva.com.

Legal Information

Sepharose is a trademark of Cytiva

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Articles

How to optimize purification of histidine-tagged proteins using Cytiva products.

This page describes principles and standard conditions for different purification techniques of histidine-tagged proteins using Cytiva products.

This page shows troubleshooting instructions for affinity chromatography of tagged proteins using Cytiva products.

This page shows the characteristics of Ni Sepharose, Ni Sepharose excel, TALON Superflow, and uncharged IMAC Sepharose products from Cytiva.

Protocols

This protocol shows how to remove histidine tags by enzymatic cleavage using Cytiva products.

This page shows how to purify histidine-tagged proteins secreted into eukaryotic cell culture supernatants using Ni Sepharose Excel from Cytiva.

This page shows how to perform sample desalting, buffer exchange and concentration for affinity chromatography of tagged proteins.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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