Amintra Protein G Resin

Amintra Protein G Resin

Amintra Protein A Resin.jpg
 
 
 
Amintra Protein G resin; a fast flow sepharose matrix covalently modified with recombinant Protein G expressed in E. coli. The albumin domain naturally present in these proteins has been deleted to create a resin with a high capacity and affinity for antibodies. Typically binding capacity of 25 mg IgG / ml resin.

Loose Resin
Protein G resin is formulated in 20% ethanol. Do not freeze the resin (freezing the suspension will damage the agarose beads), or store it at room temperature. All resins are susceptible to oxidative agents and high temperatures should be avoided. The resin is resistant to short exposure of 8M urea, pH 11 and pH 1.0. Protein G is resistant to treatment with 0.1M NaOH.
 
Specifications
 
Protein G Recombinant Protein G expressed in E. coli deficient in albumin binding domain
Supporting matrix:
4% crosslinked agarose resin
Ligand Density: 2 mg Protein G/ml resin
Bead size range:
45-165 m
Recommended working pH:
pH 2.5- 9.0
Typical binding capacity:
Upto 20 mg Human IgG /ml resin
Linear Flow rate Upto 300 cm/h (5cm diameter column, pressure 1 bar)
Maximum Flow rate 20-40 ml/min
Optimum Flow rate 1-10 ml/min
Maximum pressure 0.1MPa (1 bar)
Chemical stability: High
Solubility in water: Insoluble
Toxin Levels Free of Staphyloccocus enterotoxins and hemolysins
 
Detemine Antibody Concentration
 
For pure solution the Beer-Lambert law, A = .c.l, can be used to determine the protein concentration of IgG (mg/ml).
 
Extinction Coefficient (ml.mg-1.cm-1)
 
IgG
0.72
IgM
0.84
IgA 0.94
 
Sandwich ELISA assay can also be used to accurately measure antibody concentrations within a range of 1 mg/ml to 20 mg/ml sample. The antibodies can also be monitored for purity by SDS-PAGE under reducing or non-reducing conditions (see page xxx). Note that IgG appears in a reducing SDS-PAGE as 25 kDa and 50-55 kDa bands and IgM appears as 25 kDa and 70-80 kDa bands. Recovery of immunoglobulins can be quantified by Bradford assay (see pages 14 & 15), scanning densitometry of reducing or non-reducing SDS-polyacrylamide gels or ELISA.
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