Return to our Home Page
Novagen Home Page

Tech Resources
TB235 GST•Bind™ Kits
MSDS - English
Other Languages
Selected Citations
Store
2 to 8°C2 to 8°C
Ship
Shipped at Ambient Temperature or with Blue IceAmbient or blue ice
Note: Store and Ship conditions may differ.
See Key

His•Tag® and GST•Tag™ Fusion Protein Purification in a 96-well Format
  GST•Mag™ Agarose Beads
Cat. No. 71084  
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Purification » Purification Systems » GST•Bind™ Purification Kits
GST•Bind™ Purification Kits
Affinity purification of GST fusion proteins
 
The GST•Bind™ Purification Kits are based on the widely recognized affinity of glutathione-S-transferase fusion proteins for immobilized glutathione. 
 
Product Description

GST•Mag™ Agarose Beads are available for rapid purification of multiple samples with minimum handling time. The 3-µm (average diameter) beads have binding capacity up to 2 mg/ml of settled resin as measured with GST protein and are easily collected with a magnet, which enables binding, wash, and elution procedures to be carried out in a single tube or well.  

Need additional information about this product? Email our Technical Service department at: novatech@novagen.com

 Related information for this product is available:

EMD Chemicals Inc. list price is displayed (pricing with local distributors may vary). NOTE: In Stock status is based on item availability worldwide.

Cat. No.
Size
In Stock
Select Country Above
For Pricing Information
71084-32 × 1 mlYN/A
71084-410 × 1 mlYN/A

Related Literature:

Protein Purification and Detection Tools

pET-41 Ek/LIC Vector Kit

Material Safety Data Sheets:
71084: GST•Mag™ Agarose Beads - English
Bulgarian
Danish
Dutch
Finnish
French
German
Greek
Hungarian
Italian
Korean
Norwegian
Polish
Portuguese
Spanish
Swedish

Related Categories:
All Categories » Novagen » Protein Expression, Purification, and Detection » Protein Purification » Purification Systems » GST•Bind™ Purification Kits

Selected Citations:
  1. Jeffrey G. Gardner, et al. (2006) Control of acetyl-coenzyme A synthetase (acsA) activity by acetylation/deacetylation without NAD+ involvement in Bacillus subtilis. Journal of Bacteriology 188, 5460-5468.
  2. Vincent J. Starai, Jeffrey G. Gardner and Jorge C. Escalante-Semerena. (2005) Residue Leu641 of acetyl-CoA synthetase (Acs) is critical for the acetylation of residue Lys609 by the protein acetyltransferase (Pat) enzyme of Salmonella enterica. Journal of Biological Chemistry 280, 26200-26205.