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Protein G ResinDescription:
Protein G Resin (Cat. No. L00209) is useful for purification and isolation of IgG. Protein G, a bacterial cell wall protein isolated from group G Streptococci, binds to mammalian IgGs mainly through Fc regions. Native protein G has three IgG binding domains and other sites for albumin and cell-surface binding. Albumin and cell-surface binding domains have been eliminated from recombinant protein G to reduce nonspecific binding. Additionally, 3xCys tag has been attached to the C terminus of recombinant-protein G to facilitate its immobilization. Although the tertiary structures of proteins A and G are very similar, their amino acid compositions differ significantly, resulting in different binding characteristics. Protein G may be used for the 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 certain subclasses including human IgG3, mouse IgG1, and rat IgG2a. Unlike protein A, protein G does not bind to human IgM, IgD, or IgA.
Key Features:
- Broad IgG binding spectrum
- Binding specificity complements of protein A
- Agarose media
- No specific albumin binding
- Optimized homogeneous recombinant ligand
- High capacity
- Available in bulk
- Highly competitive price
Characteristics:
| Ligand | Recombinant Streptococcal Protein G lacking the albumin-binding produced in E. coli | | Number of IgG binding sites per ligand | 3 | | MW of ligand | Approximately 22 kDa | | PI of ligand | 4.69 | | Degree of substitution | Approximately 2 mg protein G/ml | | Static binding capacity | >20 mg sheep IgG/ml drained medium | | Stability | 37°C, 7 days | | Matrix spherical | agarose, 4% | | Average particle size | 90 μm (45–165 μm) | | Sterilization | Wash the packed column with 70% ethanol | | Storage | 20% ethanol at +4 to +8°C |
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