Weak anion exchange Fractogel^® resin featuring the tentacle technology, for purification of acidic and neutral proteins and peptides from multiple sources, pDNA purification, DNA, RNA, and endotoxin removal, large viruses purification, vaccine purification, blood fractionation, and more

Fractogel^® EMD DMAE (M) enables:

• Excellent binding to large viruses and plasmid DNA
• Homogenous binding with high selectivity and purity
• Lower elution volumes for the highest purity levels
• Compatibility with 2.5 % (v/v) aqueous benzyl alcohol containing 150 mM NaCl storage solution

Due to the titration behavior, the ion exchange capacity can be used from pH 2 to pH 9.5. The separation of proteins is based on reversible electrostatic interactions between the negatively charged regions of the proteins′ surface and the support. Proteins are retained efficiently on Fractogel^® EMD DEAE when the pH of the buffer is about 1 unit above their isoelectric points (pl).

The strength of the binding depends on the following:

• the buffer system
• pH value of the buffer which determines the surface charge of the protein
• the degree of the ionization of the functional groups of the exchanger
• the concentration of the counter ions
• the charge density on the support (protein binding capacity)

Plastic bottle

Appearance: Milky, turbid suspension,free from impurities (foreign particles)
Microscopic evaluation: Uniform spherical particles,no agglomerates, no fines
Extractable matter (water): ≤ 0.03 %
Cerium: ≤ 1 µg/g
Pressure drop(column: ID=1.6 cm, L=10 cm at 5 ml/min): ≤ 1.0 bar
Particle size (d10): 37 - 45 µm
Particle size (d50): 48 - 60 µm
Particle size (d90): 63 - 77 µm
Colony forming units (TAMC + TYMC): ≤ 100 CFU/ml
Endotoxins: ≤ 1.00 EU/ml
Protein binding capacity (bovine serum albumin): 80 - 120 mg/ml
Functional test (b:a): ≤ 0.25
Functional test: Separation of conalbumin and human serum albumin

FRACTOGEL is a registered trademark of Merck KGaA, Darmstadt, Germany