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F1879 Sigma-Aldrich

Formaldehyde Dehydrogenase from Pseudomonas sp.

lyophilized powder, 1.0-6.0 units/mg solid

Synonym: Formaldehyde:NAD+ oxidoreductase

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Properties

Related Categories 1.2.x.x Acting on aldehydes or oxo groups, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index,
Quality Level   200
form   lyophilized powder
specific activity   1.0-6.0 units/mg solid
storage temp.   −20°C

Description

General description

Formaldehyde Dehydrogenase (FDH) belongs to the medium-chain alcohol dehydrogenase family. It is encoded by the fdhA and fdhB gene in Pseudomonas aeruginosa. The FDH sequences of P. aeruginosa and P. putida are conserved and show homology. FDH exists as dimer and tetramer with zinc in their catalytic active site. The monomer corresponds to 350-400 amino-acid residues.

Application

Formaldehyde Dehydrogenase from Pseudomonas sp. has been used in standard curve generation for the demethylation-FDH assay of lysine specific demethylase 1 (LSD1) and in formaldehyde dehydrogenase (FDH) assay.

Formaldehyde dehydrogenase is used as a biosensor for the presence of formaldehyde in pharmaceuticals, waste water, vaccines and industrial products. It was also used in coupled pectin methyl esterase (PME) enzyme assay.

Packaging

5, 25, 50 units in glass bottle

Biochem/physiol Actions

Formaldehyde dehydrogenase catalyzes the conversion of formaldehyde to formate.

Formaldehyde dehydrogenases elicit protection from formaldehyde and are regarded as detoxification system.

Unit Definition

One unit will oxidize 1.0 μmole of formaldehyde to formic acid per min at pH 7.5 at 37 °C.

Physical form

Lyophilized powder containing ~70% stabilizers as Mg2+, Ca2+, bovine serum albumin, glycine, and lysine

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

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Peer-Reviewed Papers
15

References

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