Immobilized Protein G

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SKU: 786-284-XX Category:
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Description

Immobilized protein G is for binding the constant domains of immunoglobulin (Ig) molecules (see Figure 1). It is ideal for the easy one-step purification of classes, subclasses and fragments of immunoglobulins for biological fluids and cell culture media. Protein G is a modified form of Streptococcal group G so that it does not bind to albumin. Protein G is coupled to 4% highly cross-linked agarose beads by a proprietary coupling method that provides high coupling efficiency for Ig and minimal protein G leaching. Our immobilized protein G has a high binding capacity (>20mg sheep IgG/ml resin).

 

Protein G can be used for purification of mammalian monoclonal and polyclonal IgGs that do not bind well to protein A. Protein G has greater affinity than protein A for most mammalian IgGs, especially for certain subclasses including human IgG3, mouse IgG1 and rat IgG2a. Unlike protein A, protein G does not bind to human IgM, IgD and IgA.

 

The Immobilized Protein G 0.2ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples.  Each 0.2ml column enables purification of 0.1-1mg IgG from 25-500µl of serum or other sample.

 

The Immobilized Protein G 1ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples.  Each 1ml column enables purification of 1-13mg IgG from 0.5-2ml of serum or other sample.

 

Also available in 96-well spin plate formats for processing up to 96 samples.

 

Specific binding and elution buffers are also available.

 

Click here to request bulk or custom sizes.

 

 

Features

  • High binding capacity: 38mg human IgG/ml resin; >20mg sheep IgG/ml resin
  • Ligand: Recombinant Streptococcal Protein G lacking the albumin-binding domain produced in E. coli
  • Bead size: 50-165μm
  • Bead Structure: 4% highly cross-linked agarose
  • Maximum flow rate 1000cm/hr
  • Maximum pressure 300kPa

 

Applications

  • Suitable for immunoaffinity chromatography and immunoprecipitation.

 

 

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