|Catalog Number||Size||Price (USD)||Shopping Cart|
|MO22157||100 ul||$295.00||Buy Now | Add to Cart|
Aldolase A is generally considered to be a muscle enzyme. Northern analysis of cultured cells suggests that it is present in both neurons and glia. Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B.
Image: View of mixed neuron/glial cultures stained with MO22157 (green) and our rabbit antibody to NeuN/FOX3 antibody (RA22113, red). MO22157 antibody reveals strong cytoplasmic staining in astrocytes, while Rabbit Fox3/NeuN antibody shows nuclear and distal cytoplasmic staining in neuron cells and is complete absence of astrocytes. Blue is a DNA stain
Earlier studies using isozyme-specific antibodies report its location in gray matter astrocytes and cells of the pia mater. In situ hybridization of mouse central nervous system using isozyme-specific probes revealed that aldolase A and C are expressed in complementary cell types: aldolase A mRNA is found in neurons; aldolase C message is detected in astrocytes, some cells of the pia mater, and Purkinje cells. Aldolase C can in some situations be used as an astrocyte marker. However Purkinje cells of the cerebellum contain high levels of the enzyme, so the enzyme is not totally astrocyte specific.
Image: Blots of recombinant human Aldolase A, B and C with MO22156 as indicated showing binding to all three gene products. Lane labelled S show molecular weight standards, while lanes A, B and C contain recombinant full length His-tagged human Aldolase A, B and C respectively. The epitope for MO22156 is within the core of the three Aldolase molecules which are less conserved than the N and C-termini where our Aldolase C specific antibodies bind. The specificity of our other two Aldolase antibodies is shown in the indicated parts of the image. One antibody binds to the N-terminal peptide MO22135 and one to the C-terminal peptide MO22157