Skip to Content
Merck
All Photos(1)

Documents

GE17371201

Ni Sepharose Excel, 25 ML

Cytiva 17371201, 90 μm avg. part. size

Synonym(s):

Ni Sepharose Excel

Sign Into View Organizational & Contract Pricing


About This Item

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.)

Related Categories

General description

Ni Sepharose excel is an immobilized metal ion affinity chromatography (IMAC) resin precharged with nickel ions very strongly bound to a chelating ligand. This histidine-tagged (his-tagged) protein purification medium ensures minimized Ni-leakage and maximized protein recovery when samples contain stripping agents. Samples that usually cause stripping of metal ions can therefore be loaded to the medium. The nickel ions have been shown to remain bound to the chelating ligand even after incubation for 24 hours in 10 mM EDTA. Ni Sepharose excel is designed primarily for capture and purification of his-tagged proteins secreted into cell culture supernatants from eukaryotic cells such as insect cells or CHO cells by IMAC.

Ni Sepharose excel enables direct loading of samples without having to perform extensive and time-consuming pretreatment procedures. The flow properties of the medium make it excellent for purifications in a wide range of scales and allow loading of large sample volumes, enabling purification of low concentrations of target proteins at large volumes.

Features and Benefits

Ni Sepharose excel affinity media for capture and purification of histidine-tagged proteins secreted into eukaryotic cell culture supernatants by immobilized metal ion affinity chromatography (IMAC).

  • Load eukaryotic cell culture samples containing secreted histidine-tagged proteins directly with retained binding capacity
  • Increase target protein yield and decrease degradation through reduced and simplified sample handling
  • Choose between several formats for screening and preparative purification of histidine-tagged proteins

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

Pictograms

Environment

Signal Word

Warning

Hazard Statements

Storage Class Code

3 - Flammable liquids


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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

Slide 1 of 10

1 of 10

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

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

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.

Contact Technical Service