GLK-gel Affinity Chromatography Resin

Cross-linked Agarose Type

GLKgel Agarose media offer the highest specificity and selectivity in biomolecular separations and purifications. Purifications up to several orders of magnitude can be achieved in a single step. Affinity separation can often remove contaminants difficult to eliminate using conventional chromatographic procedures.

  • Uniform particle size, High resolution, Low poriness
  • High column efficiency
  • Excellent bonding and end-capping technologies
packing material for HPLC column



Pr A 4FF

Pr G 4FF IgM 6HP



4% cross-linked agarose

6% cross-linked agarose


rProtein A

rProtein G IgM


Particle Size

90µm (45-165µm)

37µm (25-45µm)


20mg hIgG/ml

25mg hIgG/ml 5mg hIgG/ml

20mg hIgG/ml

pH Stability

2-10 (Short)   3-9 (Long)

2-13 (Short)   3-11 (Long)

Max. Pressure


Flow Rate


300cm/h 150cm/h



4-8 °C, 20% EtOH

Alkaline-resistant Agarose Protein A

Items Performance
Matrix Highly cross-linked agarose particles
Average particle size ~60µm
Ligand Super alkaline resistant Protein A
Combined loading Capacity* > 80 mg hlgG/ml media
Chemical stability Common reagents used in the purification of tolerable antibodies
Working pH 3-10
Clean-in-Place 0.1-0.5 M NaOH
Recommended linear flow rate 100-500 cm/h
Save 1XPBS with 20% ethanol, 2-8℃

*Note: The dynamic binding capacity of the target antibody needs to be determined by front-end analysis using the actual sample. The dynamic binding load is a function of the retention time of the sample and therefore needs to be defined over a range of retention times of the sample.


Purification of IgG in human serum

  • Sample: 5ml human serum with five times dilution (different buffers)
  • Column: HT01 1.0ml Protein G 4FF
  • BalanceA 0.02 M PB pH7.0; B 0.02M PB, 0. 3M NaCl pH 7.0
  • Elution: 0.1 M Glycine-HCl pH2.7
  • Flow Rate: 0.25m/min (sampling), 1ml/min
agarose affinity application

Protein Purification

agarose affinity application

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There are plenty of manufacturers in chromatography resin market. But, we are the

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