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Description

Application: L-Phenylalanine-Separopore® 4B-CL is used for the purification of phenylalanine binding proteins, such as phenylalanine hydroxylase.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References

The purification and characterization of a cysteine protease of Fasciola gigantica adult worms. Vet Parasitol. (1992) 43: 223-32.
Mechanism of inactivation of a Fasciola proteolytic enzyme by peptide aldehydes and alkylating agents. Mol Biochem Parasitol. (1983) 8: 89-97.
Hemoglobinolytic activity of serum in mice infected with Schistosoma mansoni. Am J Trop Med Hyg. (1981) 30: 96-101.
Extracellular fibrinogenolytic enzyme of Aspergillus fumigatus: substrate-dependent variations in the proteinase synthesis and characterization of the enzyme. FEMS Immunol Med Microbiol. (1993) 7: 81-91.
Zymographic analysis of extracellular, released and cell-associated proteases of rat interleukin 2-activated natural killer (A-NK) cells. In Vivo. (1994) 8: 33-41.

Properties

Storage Temperature

2-8°C

ECCN #

EAR99

Matrix

Separopore® 4B-CL (crosslinked agarose beads, 4%)

Particle Size Range

52 - 165 μm

Matrix Activation

Cyanogen bromide

Matrix Attachment

Amino group

Spacer Arm

8 atoms (aminocaproic acid)

Suspension/Column/Cartridge

Supplied as a suspension in 1M NaCl, 0.02% thimerosal

pH Stability

3 - 10

Flow Specifications

70 - 140 cm / h

Molecular Weight Range

6 x 104 - 2 x 107

Extent of Coupling

2 - 10 μmol / ml