Background:  Aldolase B is a tetrameric glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Fructose 1,6-bisphosphate aldolase catalyses the reversible condensation of glycerone-P and glyceraldehyde 3-phosphate into fructose 1,6-bisphosphate. Fructose 1,6-bisphosphate aldolase exists as three forms, the muscle-specific Aldolase A, the liver-specific aldolase B, and the brain-specific aldolase C. Aldolase A, B, and C arose from a common ancestral gene, from which aldolase B first diverged. Aldolase A is one of the most highly conserved enzymes known, with only about 2% of the residues changing per 100 million years. Aldolase B is regulated by the hormones insulin and glucagon and has been implicated in hereditary fructose intolerance disease. Aldolase C is a polypeptide that is exclusively expressed in Purkinje cells. Aldolase C-positive Purkinje cells are organized in the cerebellum as stripes or bands that run from anterior to posterior across the cerebellum and alternate with bands of Aldolase C-negative Purkinje cells.

Description: Rabbit polyclonal to Aldolase B

Immunogen: KLH conjugated synthetic peptide derived from Aldolase B

Specificity:  ·Reacts with Human, Mouse, Pig and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 39 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.