A2714
Aldolase from rabbit muscle
lyophilized powder, ≥8.0 units/mg protein
동의어(들):
D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
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
Quality Level
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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 .
Physical form
Essentially sulfate-free containing citrate buffer salts
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.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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
Lara Babich et al.
ChemSusChem, 5(12), 2348-2353 (2012-11-15)
Herein, we report a new flow process with immobilized enzymes to synthesize complex chiral carbohydrate analogues from achiral inexpensive building blocks in a three-step cascade reaction. The first reactor contained immobilized acid phosphatase, which phosphorylated dihydroxyacetone to dihydroxyacetone phosphate using
N C Cross et al.
Lancet (London, England), 335(8685), 306-309 (1990-02-10)
The molecular basis of hereditary fructose intolerance (HFI) was studied in 50 subjects (41 pedigrees, 82 apparently independent mutant alleles of aldolase B) by direct analysis of aldolase B genes amplified by means of the polymerase chain reaction. The mutation
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