catalog number :
MBS415126
products full name :
ALDOC Antibody
products short name :
ALDOC
products name syn :
ALDOC
other names :
ALDOC; Fructose-bisphosphate aldolase C; fructose-bisphosphate aldolase C; aldolase 3; fructoaldolase C; brain-type aldolase; fructose-1,6-biphosphate triosephosphate lyase; aldolase C, fructose-bisphosphate; Brain-type aldolase
products gene name :
ALDOC
other gene names :
ALDOC; ALDOC; ALDC; ALDC
uniprot entry name :
ALDOC_HUMAN
purity :
Affinity purified
concentration :
100ug/100ul
storage stability :
Store at -20 degree C/1 year
tested application :
Immunofluorescence (IF), Western Blot (WB)
app notes :
The antibody solution can be used at dilutions 1:500-1:1,000 for immunofluorescence. For western blots try at 1:1,000-2,000.
other info1 :
Immunogen: Aldolases are glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose 1,6-bisphosphate and fructose-1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Three aldolase isozymes are found in mammals specifically aldolases A, B, and C, each of which is encoded by a separate gene. 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 (1). Aldolase B is considered to be a liver-specific enzyme and it is transcriptionally activated by signals from hormones and dietary factors (2). In the adult, aldolase C is the brain-specific isozyme, with low but detectable activity in fetal tissues (1, 3-6). Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B. Earlier studies using isozyme-specific antibodies report its location in gray matter astrocytes and cells of the pia mater (5, 8). 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 (9). 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. MBS415126 was raised against N-terminal 20 amino acids of aldolase C protein, the sequence MPHSYPALSAEQKKELSDIA. The HGNC name for this protein is ALDOC.
other info2 :
Storage Buffer: PBS, pH 7.4 with 0.02% sodium azide.
products references :
References:1. Popovici T, Berwald-Netter Y, Vibert M, Kahn A, Skala H. Localization of aldolase C mRNA in brain cells. FEBS Lett. 268, 189-193 (1990).2. Weber A, Marie J, Cottereau D, Simon M, Besmond C, Dreyfus J. & Kahn A. Dietary Control of Aldolase B and L-type Pyruvate Kinamse RNAs in Rat. J. Biol. Chem 259, 1798-1802 (1984).3. Mukai T, Yatsuki H, Masuko S, Arai Y, Joh K & Hori K. The structure of the brain-specific rat aldolase C gene and its regional expression. Biochem. Biophys. Res. Commun. 174, 1035-1042 (1991).4. Royds J, Ironside J, Warnaar S, Taylor C & Timperle W. Monoclonal antibody to aldolase C: a selective marker for Purkinje cells in the human cerebellum. Neuropathol. Appl. Neurobiol. 13, 11-21(1987).5. Thompson R., Kynoch P. Willson V. Cellular localization of aldolase C subunits in human brain. Brain Res. 232, 489-493 (1982).6. Schapira F, Reuber M, Hatzfeld A. Resurgence of two fetal-type of aldolases (A and C) in some fast-growing hepatomas. Biochem. Biophys. Res. Commun. 40, 321-327(1970).7. Arai Y, Kajihara S, Masuda J, Ohishi S, Zen K, Ogata J. Mukai T. Position-independent, high-level, and correct regional expression of the rat aldolase C gene in the central nervous system of transgenic mice. Eur. J. Biochem. 221, 253-260 (1994).8. Wachsmuth E, Thorner M. & Pfleiderer G. The cellular distribution of aldolase isozymes in rat kidney and brain determined in tissue sections by the immuno-histochemical method. Histochemistry, 45, 143-161 (1975).9. Walther EU, Dichgans M, Maricich SM, Romito RR, Yang F, Dziennis S, Zackson S, Hawkes R, Herrup K. Genomic sequences of aldolase C (Zebrin II) direct lacZ expression exclusively in non-neuronal cells of transgenic mice. Proc Natl Acad Sci U S A. Mar 3;95(5):2615-20(1998).
ncbi acc num :
CAG46679.1
ncbi mol weight :
39,456 Da
ncbi pathways :
Biosynthesis Of Amino Acids Pathway (790012); Biosynthesis Of Amino Acids Pathway (795174); Carbon Metabolism Pathway (814926); Carbon Metabolism Pathway (817567); Conversion Of Glucose To Acetyl CoA And Entry Into The TCA Cycle Pathway (835393); Fructose And Mannose Metabolism Pathway (82930); Fructose And Mannose Metabolism Pathway (291); Gluconeogenesis Pathway (106204); Gluconeogenesis, Oxaloacetate = Fructose-6P Pathway (413342); Gluconeogenesis, Oxaloacetate = Fructose-6P Pathway (468196)
ncbi summary :
This gene encodes a member of the class I fructose-biphosphate aldolase gene family. Expressed specifically in the hippocampus and Purkinje cells of the brain, the encoded protein is a glycolytic enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehyde, respectively. [provided by RefSeq, Jul 2008]
uniprot summary :
Catalytic activity: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.14. Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Subunit structure: Homotetramer. Interacts with ATP6V1E1. May interact with PLD2. Ref.10 Ref.11. Miscellaneous: In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain. Sequence similarities: Belongs to the class I fructose-bisphosphate aldolase family. Biophysicochemical propertiesKinetic parameters:KM=10.7 uM for fructose 1,6-bisphosphate Ref.14KM=16 mM for fructose 1-phosphate. Sequence caution: The sequence AAI03761.1 differs from that shown. Reason: Erroneous initiation.