Akr1c21 Antibodies

AND Akr1c21 ELISA kits, Akr1c21 Proteins

Many biological assays use antibodies to detect Akr1c21, such as Western Blot (WB), ELISA, Flow Cytometry, Immunocytochemistry (IHC). These antibodies can be polyclonal or monoclonal, and react with Akr1c21 in Human, Mouse, Rat, and many other animal samples. Boster Bio use mainly mouse and rabbit to develop Akr1c21 antibodies...

We validate the specificity of these antibodies to Akr1c21 by testing them on tissues known to express Akr1c21 positively and negatively. Browse below to find the Akr1c21 antibody that suites your experiment. We have 0 of these antibodies and many publications and validation images.

If you cannot find antibodies that fit your needs, contact us for making custom antibodies. We have a full suite of custom antibody services covering from research to diagnostic and therapeutic applications.

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Akr1c21 Infographic by Boster Bio

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Akr1c21 Overview

Facts about Aldo-keto reductase family 1 member C21.

Akr1c21 3D structure. Source: alphafold

Aldo-keto reductase family 1 member C21 (Akr1c21)

NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione to androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity.

Has broad substrate specificity and acts on different 17-alpha- hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3- ketosteroids. Reduction of keto groups is strictly stereoselective.

Gene Information

Mouse
Gene Name:	Akr1c21
Uniprot:	Q91WR5
Entrez:	77337

Family

Belongs to:

aldo/keto reductase family

Alternative Names

Aldo-keto reductase family 1 member C21

Molecular Weight

Mass (kDA):
36.877 kDA

Genomic Context


Mouse

Location:	13\|13 A1
Sequence:	13;

Tissue Specificity

Detected in kidney and brain.

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/Akr1c21

References

PMID: 15577209 by Ishikura S., et al. Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase family.

PMID: 16018803 by Bellemare V., et al. Characterization of 17alpha-hydroxysteroid dehydrogenase activity (17-alpha-HSD) and its involvement in the biosynthesis of epitestosterone.