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MAK223

Sigma-Aldrich

Aldolase Activity Colorimetric Assay Kit

Sufficient for 100 Colorimetric tests

Sinónimos:

Aldolase Colorimetric Assay Kit

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.84

detection method

colorimetric

relevant disease(s)

cancer; neurological disorders; hematological disorder

storage temp.

−20°C

Gene Information

human ... ALDOA(226) , ALDOB(229) , ALDOC(230)
mouse ... ALDOA(11674) , ALDOB(230163) , ALDOC(11676)
rat ... ALDOA(24189) , ALDOB(24190) , ALDOC(24191)

General description

Aldolase (fructose-bisphosphate aldolase; EC 4.1.2.13) catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three isoforms of aldolase (A, B, and C) are differentially expressed during development. Aldolases have been recognized as positive regulators of the Wnt signaling pathway. Deficiency of aldolases is associated with myopathy and hemolytic anemia.

The Aldolase Activity Colorimetric Assay Kit is a simple and high throughput assay for measuring aldolase activity in serum, plasma, and a variety of tissues and cells. Aldolase activity is determined by measuring a colorimetric product with absorbance at 450 nm (A450) proportional to the enzymatic activity present. One unit of aldolase is the amount of enzyme that generates 1.0 μmole of NADH per minute at pH 7.2 at 37 °C.
Aldolase (fructose-bisphosphate aldolase; EC 4.1.2.13) catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three isoforms of aldolase (A, B, and C) are differentially expressed during development. Aldolases have been recognized as positive regulators of the Wnt signaling pathway. Deficiency of aldolases is associated with myopathy and hemolytic anemia

Features and Benefits

Compatible with high-throughput handling systems.

Suitability

Suitable for the detection of Aldolase activity in biological samples such as tissue, cells, serum, and plasma.

Principle

The Aldolase Activity Colorimetric Assay Kit is a simple and high throughput assay for measuring aldolase activity in serum, plasma, and a variety of tissues and cells. Aldolase activity is determined by measuring a colorimetric product with absorbance at 450 nm (A450) proportional to the enzymatic activity present. One unit of aldolase is the amount of enzyme that generates 1.0 μmole of NADH per minute at pH 7.2 at 37 °C.

Solo componentes del kit

Referencia del producto
Descripción
  • Aldolase Assay Buffer
  • Aldolase Substrate
  • Aldolase Enzyme Mix
  • Aldolase Developer
  • NADH Standard
  • Aldolase Positive Control

pictograms

Corrosion
GHS05

signalword

Danger

hcodes

H314,H412

Hazard Classifications

Aquatic Chronic 3 - Eye Dam. 1 - Skin Corr. 1B

Storage Class

8A - Combustible corrosive hazardous materials

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Aldolase positively regulates of the canonical Wnt signaling pathway.
Caspi M, et al.
Molecular Cancer, 13(1), 164-164 (2014)
Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function.
Esposito G, et al.
The Biochemical Journal, 380(1), 51-56 (2004)
Unraveling the structural and functional features of an aldolase A mutant involved in the hemolytic anemia and severe rhabdomyolysis reported in a child.
Esposito G, et al.
Blood, 105(2), 905-906 (2005)
Zhenchang Guo et al.
Molecular & cellular proteomics : MCP, 20, 100053-100053 (2021-02-10)
Esophageal squamous cell carcinoma (ESCC) is an aggressive malignancy with poor therapeutic outcomes. However, the alterations in proteins and posttranslational modifications (PTMs) leading to the pathogenesis of ESCC remain unclear. Here, we provide the comprehensive characterization of the proteome, phosphorylome
Biochemical markers of muscular damage.
Brancaccio P, et al
Clinical Chemistry and Laboratory Medicine, 48(6), 757-767 (2010)
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