Purified pectin with acidophilus

Pectolyase Y-23 is a highly purified maceration enzyme from Aspergillus niger. It contains two types of pectinase such as endopolygalacturonase and endo-pectin lyase in high activity.

Pectolyase Y-23 is a highly purified maceration enzyme from Aspergillus niger. It contains two types of pectinase such as endopolygalacturonase and endo-pectin lyase in high activity.

General description This substance is supplied with certified chromatographic purity. The exact value can be found on the certificate.

Features Ultrapure qualityAgglutinates leucocytes and erythrocytesMixture of L and E subunitsSugar specificity: complex oligosaccharidesLyophilized powderProduct descriptionPhaseolus vulgaris lectin P or Phytohemagglutinin (PHA-P)is isolated from

Features Ultrapure qualityAgglutinates leucocytes and erythrocytesMixture of L and E subunitsSugar specificity: complex oligosaccharidesLyophilized powderProduct descriptionPhaseolus vulgaris lectin P or Phytohemagglutinin (PHA-P)is isolated from

Features Ultrapure qualityAgglutinates leucocytes and erythrocytesMixture of L and E subunitsSugar specificity: complex oligosaccharidesLyophilized powder Product descriptionPhaseolus vulgaris lectin P or Phytohemagglutinin (PHA-P)is isolated from

Features Ultrapure qualityAgglutinates leucocytes and erythrocytesMixture of L and E subunitsSugar specificity: complex oligosaccharidesLyophilized powder Product descriptionPhaseolus vulgaris lectin P or Phytohemagglutinin (PHA-P)is isolated from

Crude Phaseolus vulgaris-P lectin (PHA-P) from the Red Kidney Bean. Phytohemagglutinin PHA agglutinates the erythrocytes of all human blood groups as well as those of rabbit, dog, cat, mouse, sheep, and guinea pig.

PHA-L is purified from Phaseolus vulgaris (red kidney bean) by standard chromatographic techniques. Phytohemagglutinin (PHA), the lectin extract from the red kidney bean, consists of only L-type subunits (isolectin L4, leuko-agglutinin).""

PUE 7.1 Terminal

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues: the other is related to the 8-anilinonaphthalene-1-sulfonate binding. Application:An experimental approach using SDS-PAGE, in-gel trypsin

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues: the other is related to the 8-anilinonaphthalene-1-sulfonate binding. Application:An experimental approach using SDS-PAGE, in-gel trypsin