A2714
Aldolase from rabbit muscle
lyophilized powder, ≥8.0 units/mg protein
Synonym(s):
D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-781-0
MDL number:
Specific activity:
≥8.0 units/mg protein
Biological source:
rabbit muscle
biological source
rabbit muscle
form
lyophilized powder
specific activity
≥8.0 units/mg protein
composition
Protein, ≥80% biuret
foreign activity
glyceraldehyde-3-phosphate dehydrogenase ≤0.03%, lactic dehydrogenase ≤0.03%, phosphoglucose isomerase ≤0.6%, pyruvate kinase ≤0.1%, triosephosphate isomerase ≤0.05%
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
Application
Aldolase is used to convert fructose 1,6-diphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Aldolase, from rabbit muscle has been used for stereospecific deprotonation at DHAP C3 . Product A2714 is essentially sulfate-free and contains citrate buffer salts.
Biochem/physiol Actions
Aldolase is involved in gluconeogenesis, the Calvin cycle and glycolysis. Aldolase, from rabbit muscle, is a class I aldolase which forms covalent Schiff base intermediates. The active site of aldolase is in the center of the α/β 8 barrel fold .
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.
Physical form
Essentially sulfate-free containing citrate buffer salts
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Clotilde LowKam et al.
The Journal of biological chemistry, 285(27), 21143-21152 (2010-04-30)
Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the reversible cleavage of four
Bang Shen et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(9), 3567-3572 (2014-02-20)
Gliding motility and host-cell invasion by apicomplexan parasites depend on cell-surface adhesins that are translocated via an actin-myosin motor beneath the membrane. The current model posits that fructose-1,6-bisphosphate aldolase (ALD) provides a critical link between the cytoplasmic tails of transmembrane
Xiaochen He et al.
Journal of cellular physiology, 237(8), 3317-3327 (2022-05-28)
Hypertension is an important risk factor in the pathogenesis of diastolic dysfunction. Growing evidence indicates that glucose metabolism plays an essential role in diastolic dysfunction. TP53-induced glycolysis and apoptosis regulator (TIGAR) has been shown to regulate glucose metabolism and heart
Tiia Kittilä et al.
Chembiochem : a European journal of chemical biology, 17(7), 576-584 (2016-01-12)
Nonribosomal peptide synthetases (NRPSs) produce many important and structurally complex natural products. Because of their architectures, reprogramming NRPSs has long been attempted to access new bioactive compounds. However, detailed characterization of NRPS catalysis and substrate selectivity by adenylation (A) domains
Peter M Fernandes et al.
The Biochemical journal, 477(22), 4425-4441 (2020-11-04)
6-Phosphofructokinase-1-kinase (PFK) tetramers catalyse the phosphorylation of fructose 6-phosphate (F6P) to fructose 1,6-bisphosphate (F16BP). Vertebrates have three PFK isoforms (PFK-M, PFK-L, and PFK-P). This study is the first to compare the kinetics, structures, and transcript levels of recombinant human PFK
Related Content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service