Active, purified recombinant protein
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11β-Hydroxysteroid Dehydrogenase (human, recombinant)

Item No. 10007815

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • 11β-HSD1
  • HSD11β
Purity
≥40% estimated by SDS-PAGE
Source
Active recombinant N-terminal His-tagged protein, expressed in E. coli
MW
31.4 kDa
Formulation (Request formulation change)
50 mM Potassium phosphate pH 7.6, with 5% glycerol, 50 mM sodium chloride, 1 mM EDTA, and 0.1 mM DTT
UniProt Accession №
P28845
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    100 µg

    $534

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    Product Description

    11β-Hydroxysteroid dehydrogenase (11β-HSD) exists as two isozymes 11β-HSD1 and 11β-HSD2.1 Both isoforms are members of the short-chain dehydrogenase/reductase (SDRs) family.2 11β-HSD1 is a membrane-bound glycoprotein localized on the endoplasmic reticulum. The main catalytic domain of 11β-HSD1 lies within the lumen of the ER. A short five amino acid N-terminal region extends into the cytoplasm and is linked to the catalytic portion through a single transmembrane helix.1 11β-HSD1 is a relatively low affinity NADP-dependent enzyme with a bidirectional catalytic activity. The dehydrogenase reductase activity of 11β-HSD1 catalyzes the conversion of cortisol to cortisone. The primary function of 11β-HSD1 is the oxoreduction of cortisone to the active glucocorticoid cortisol.2 Cortisol is a steroid hormone essential for a variety of physiological and homeostatic functions.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Walker, E.A., Clark, A.M., Hewison, M., et al. Functional expression, characterization, and purification of the catalytic domain of human 11-β-hydroxysteroid dehydrogenase type 1. The Journal of Biological Chemisty 276(24), 21343-21350 (2001).

    2. Blum, A., Martin, H.J., and Maser, E. Human 11β-hydroxysteroid dehydrogenase type 1 is enzymatically active in its nonglycosylated form. Biochem. Biophys. Res. Commun. 276(2), 428-434 (2000).