TH-Protein L is a novel affinity medium synthesized by epoxidation of a certain base-resistant Protein L with a highly rigid agarose substrate, with an optimized pore size that facilitates the increase of antibody binding load. The medium is suitable for binding the variable region of the kappa light chain of the antibody, and is suitable for capturing a wide range of antibody fragments such as Fabs, single-chain variable fragments (scFv) and antibody domains (dAbs).
The ligand of TH-Protein L is a genetically engineered recombinant protein L fragment with a certain degree of alkali resistance, and the ligand fermentation and subsequent purification processes are performed without any animal-derived materials. The medium can be cleaned in situ with 15 mM NaOH, avoiding the use of expensive and corrosive in situ cleaning reagents, which can effectively save costs. Meanwhile, TH-Protein L has a higher relative loading capacity, so that a smaller column volume can be selected to reduce the cost of production during the process of scaling up.
The medium has the following characteristics:
- Highly rigid agarose base frame for fast flow rates for increased productivity.
- Highly specific kappa light chains for efficient capture of a broad selection of antibodies and antibody fragments.
- High loading capacity reduces process time and media usage, resulting in lower production costs and increased productivity.
Specifications:
Product |
TH-Protein L |
Appearance |
White slurry, forms visible layering upon standing |
Functional Group |
Protein L (from E. coli) |
Avg. Particle Size |
Approx. 80 µm |
Dynamic Binding |
Approx. 40 mg/mL human IgG/medium |
Crosslinking Mode |
Epoxy chemical |
Max. Pressure Tolerance |
0.5 MPa |
Chemical Stability |
Stable in common aqueous solutions: 10mM HCl, 0.1 M citric acid (pH=3.0), 6M guanidine hydrochloride, 6M urea, 30% isopropanol, 20% ethanol |
Pressure Flow Rate |
≥300 cm/h (TK-EC 300, h=20cm) |
pH Stability |
2–10 (operating), 15 mM NaOH (CIP) |
Recommended Flow Rate |
60–300 cm/h |