Blue Trisacryl M dye-affinity chromatography sorbent is used for the purification of a wide variety of enzymes and proteins such as kinases, interferons, and some coagulation factors. It is also used for albumin purification or albumin depletion in samples for proteomics research.
Blue Trisacryl M sorbent is based on Trisacryl GF2000 support, a macroporous non ionic synthetic polymer on which Cibacron blue 3GA is covalently immobilized through a stable six-carbon spacer arm to prevent leakage of the dye in normal working conditions.
Features and Benefits
Unique multi-modal interaction mechanism
Strong bond of dye-to-sorbent prevents leakage of the dye
Multiple laboratory to production scale applications
Presentation and Storage
Blue Trisacryl M sorbent is available as ready-to-use labpacks suspended in 1 M sodium chloride with 20% (v/v) ethanol as bacteriostatic, or in drums for process-scale applications.
For fast screening laboratory applications, the sorbent is available in 1 mL AcroSep™ column (1.48 cm bed height x 0.94 cm bed diameter). This dark blue color coded column has threaded female luer lock inlets and rotating male luer locking hub outlets, and can be easily operated using a syringe or a pump.
Blue Trisacryl M Sorbent can be Used for the Purification of Many Proteins
Blue Trisacryl M sorbent is a group-specific adsorbent with affinity for a wide variety of enzymes. Some proteins interact biospecifically with the dye due to its structural similarity with nucleotide cofactors (ADP, NADP). Other proteins like albumin or interferon bind by a combination of hydrophobic, electrostatic and pi-pi interactions.
Applications include :
Enzymes which need NAD as cofactor (kinases, dehydrogenases, phosphatases…)
Other enzymes (sulfatases, RNA polymerases, mono-oxygenases, oxydoreductases)
Column: 1.6 cm I.D. x 10 cm ; Buffer: 0.05 M Tris-HCl, pH 8.8. Elution by an NaCl gradient from 0 to 3 M.
Example II. Automatic Separation of Human Albumin from Plasma by Step Elution
Column: 2.5 cm I.D. x 6 cm; Adsorption buffer: 0.05 M Tris-HCl, 0 5 M NaCI, pH 8; Albumin elution buffer: 2.5 M NaCl in the same buffer; Regeneration solution: water-ethylene glycol mixture (50:50). —— UV absorbance at 280 nm. - — - lonic strength. - - - - pH.
Example III Depletion of Albumin From Human Plasma Using AcroSep™ Columns
L = Load, FT = Flowthrough, E = Elution. Albumin is bound to Blue Trisacryl M sorbent in 20 mM PBS buffer, pH 7.2 and eluted by an NaCl gradient from 0 to 3 M
The chemical stability of Blue Trisacryl M sorbent is a function of the synthetic nature of Trisacryl matrix and the enhanced stability of the ligand coupling mechanism. The sorbent can be operated up to 3 bar backpressure while maintaining good flow rate properties.
The binding capacity of Blue Trisacryl M sorbent depends on the protein, the composition of the feedstock and parameters such as pH. Note that the capacity for a given protein may differ according to the animal species (for example, the binding capacity for bovine albumin is lower than for human albumin).