While the total molecular weight of aldolase is reported to be 160 kDa, this enzyme has not been tested for use as a molecular weight marker. Suitability would have to be determined by the end users.
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A2714
Aldolase from rabbit muscle
lyophilized powder, ≥8.0 units/mg protein
Synonim(y):
D-Fructose-1,6-bisphosphate-D-glyceraldehyde-3-phosphate-lyase, Fructose-diphosphate Aldolase
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| Rozmiar/SKU | Dostępność | Cena netto |
|---|---|---|
100 units | Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności | 236,00 zł |
200 units | Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności | 348,00 zł |
500 units | Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności | 700,00 zł |
Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-781-0
MDL number:
Numer WE:
Specific activity:
≥8.0 units/mg protein
Biological source:
rabbit muscle
236,00 zł
Skontaktuj się z Obsługą Klienta, aby uzyskać informacje na temat dostępności
Pomoc techniczna
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Pozwól nam pomócbiological source
rabbit muscle
Quality Segment
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
Application
Biochem/physiol Actions
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.
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Ta pozycja | |||
|---|---|---|---|
| description lyophilized powder, ≥8.0 units/mg protein | description ammonium sulfate suspension, 10-20 units/mg protein | description Type X, lyophilized powder, ≥3,500 units/mg protein | description Type III-S, ammonium sulfate suspension, ≥4,000 units/mg protein |
| biological source rabbit muscle | biological source rabbit muscle | biological source - | biological source rabbit muscle |
| specific activity ≥8.0 units/mg protein | specific activity 10-20 units/mg protein | specific activity ≥3,500 units/mg protein | specific activity ≥4,000 units/mg protein |
| form lyophilized powder | form ammonium sulfate suspension | form lyophilized powder | form ammonium sulfate suspension |
| storage temp. −20°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. 2-8°C |
| Quality Level 300 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| foreign activity glyceraldehyde-3-phosphate dehydrogenase ≤0.03%, triosephosphate isomerase ≤0.05%, phosphoglucose isomerase ≤0.6%, pyruvate kinase ≤0.1%, lactic dehydrogenase ≤0.03% | foreign activity glyceraldehyde-3-phosphate dehydrogenase ≤0.03%, phosphoglucose isomerase ≤0.6%, pyruvate kinase ≤0.1%, lactic dehydrogenase ≤0.03%, triosephosphate isomerase ≤0.05% | foreign activity pyruvate kinase, lactic dehydrogenase, 3-phosphoglyceric phosphokinase, phosphoglucose isomerase, α-glycerophosphate dehydrogenase, aldolase and glyceraldehyde-3-phosphate dehydrogenase ≤0.01% | foreign activity pyruvate kinase, lactic dehydrogenase, phosphoglucose isomerase, α-glycerophosphate dehydrogenase and aldolase ≤0.001%, glyceraldehyde-3-phosphate dehydrogenase ≤0.01%, 3-phosphoglyceric phosphokinase ≤0.01% |
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Klasa składowania
11 - Combustible Solids
Co się dzieje?
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
PPE (środki ochrony indywidualnej)
Eyeshields, Gloves, type N95 (US)
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Can this product be used as the protein molecular weight standard (representing 160kDa) in the SEC chromatography analysis?
1 answer-
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What is the molecular weight (MW) of the product?
1 answer-
The molecular weight of aldolase from rabbit muscle is 161,000 daltons, and it is a tetramer composed of subunits of 40,000 daltons. This information is detailed in the research article: "The molecular weight of rabbit muscle aldolase and the properties of the subunits in acid solution" by Sia, C.L., and Horecker, B.L., published in the Arch. Biochem. Biophys. journal, volume 123, issue 1, pages 186-194 in 1968.
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