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H1506

Sigma-Aldrich

3α-Hydroxysteroid Dehydrogenase from Pseudomonas testosteroni

≥15 units/mg protein

Synonym(s):

3α-Hydroxysteroid:NAD(P)+ oxidoreductase

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About This Item

CAS Number:
9028-56-2
Enzyme Commission number:
1.1.1.50 (BRENDA, IUBMB)
EC Number:
232-839-5
MDL number:
MFCD00130298
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Pseudomonas testosteroni)

form

lyophilized solid

specific activity

≥15 units/mg protein

purified by

chromatography

composition

Protein, ≥25%

foreign activity

β-hydroxysteroid dehydrogenase ≤0.5%
alcohol dehydrogenase ≤0.05%

storage temp.

−20°C

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Application

3α-Hydroxysteroid Dehydrogenase from Pseudomonas testosterone has been used:
  • in the preparation of composite electrode platform to for the determination of androsterone
  • in potassium phosphate buffer for the bioluminescent assay of bile acids in serum
  • for total bile salts assay using an enzymatic method

Biochem/physiol Actions

3α-hydroxysteroid dehydrogenase (3α-HSD) may help to modulate the occupancy of the androgen receptor (AR) in androgen target tissues. It may also act in hindering androgen action.

Unit Definition

One unit will oxidize 1.0 μmole of androsterone per min at pH 8.9 at 25 °C in the presence of β-NAD+.

Physical form

Lyophilized powder containing potassium phosphate buffer salt, EDTA, and DL-dithiothreitol

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Experimentally determined protein tertiary structures are rapidly accumulating in a database, partly due to the structural genomics projects. Included are proteins of unknown function, whose function has not been investigated by experiments and was not able to be predicted by
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Two novel lactones, Cephalosporolides H (1) and 1 (2), were isolated from the lyophilized culture broth of the marine-derived fungus, Penicillium sp. The structures were elucidated on the basis of extensive 1D- and 2D-NMR, as well as HRESI-MS spectroscopic analyses.
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Identification of cellular targets pertinent for the development of effective therapies against pathological pain constitutes a difficult challenge. We combined several approaches to show that 3alpha-hydroxysteroid oxido-reductase (3alpha-HSOR), abundantly expressed in the spinal cord (SC), is a key target, the
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