A9329
Aldolase from spinach
lyophilized powder, 0.3-1.0 units/mg protein
Synonym(s):
D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase
form
lyophilized powder
specific activity
0.3-1.0 units/mg protein
shipped in
dry ice
storage temp.
−20°C
General description
Aldolase exists in three isoforms namely: ALDOA, ALDOB, and ALDOC. These isoenzymes are differentially expressed in human tissues.
Application
Aldolase from spinach has been used as a standard in electrophoresis for the detection of mesocarp and seed aldolase proteins.
Biochem/physiol Actions
Aldolase catalyzes the conversion of fructose 1,6-bisphosphate (F1,6BP) to glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). It plays a vital role in metabolism and glycolysis. Other than glycolytic enzymes, aldolase also interacts with F-actin, α-tubulin, dynein light chain 8, nexin 9, and phospholipase D2, which indicates its role as a scaffolder and modulator of protein complexes. In addition, it also regulates cell morphology and acidic vesicle trafficking by directly interacting with the ADP-ribosylation factor nucleotide site opener (ARNO). Aldolase may also be involved in the formation of mannoheptulose and perseitol. Increased expression of the protein has been observed in various diseases and cancer types.
Analysis Note
Crude
Protein determined by Lowry
Other Notes
One unit will convert 1.0 μmole of fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate per min at pH 7.4 at 25 °C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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D-mannoheptulose and perseitol in `Hass? avocado: Metabolism in seed and mesocarp tissue
Tesfay SZ , et al.
Southern Medical Journal, 79, 159-165 (2012)
Yu-Chan Chang et al.
Trends in endocrinology and metabolism: TEM, 29(8), 549-559 (2018-06-17)
The aldolase family members involved in metabolism and glycolysis are present in three isoforms: ALDOA, ALDOB, and ALDOC. Aldolases are differentially expressed in human tissues, and aberrant expression has been observed in several human diseases and cancer types. However, non-enzymatic
Aldolase directly interacts with ARNO and modulates cell morphology and acidic vesicle distribution.
Maria Merkulova et al.
American journal of physiology. Cell physiology, 300(6), C1442-C1455 (2011-02-11)
Previously, we demonstrated that the vacuolar-type H(+)-ATPase (V-ATPase) a2-subunit functions as an endosomal pH sensor that interacts with the ADP-ribosylation factor (Arf) guanine nucleotide exchange factor, ARNO. In the present study, we showed that ARNO directly interacts not only with
Structure- and ligand-based structure-activity relationships for a series of inhibitors of aldolase.
Leonardo G Ferreira et al.
Current computer-aided drug design, 8(4), 309-316 (2012-06-28)
Aldolase has emerged as a promising molecular target for the treatment of human African trypanosomiasis. Over the last years, due to the increasing number of patients infected with Trypanosoma brucei, there is an urgent need for new drugs to treat
Karina Rodrigues Lorenzatto et al.
Gene, 506(1), 76-84 (2012-07-04)
Glycolytic enzymes, such as fructose-bisphosphate aldolase (FBA) and enolase, have been described as complex multifunctional proteins that may perform non-glycolytic moonlighting functions, but little is known about such functions, especially in parasites. We have carried out in silico genomic searches
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