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Item number | Size | Datasheet | Manual | SDS | Delivery time | Quantity | Price |
---|---|---|---|---|---|---|---|
ELK-ES7844.50 | 50 µl | - | - |
Request delivery time estimate |
169.00€
|
||
ELK-ES7844.100 | 100 µl | - | - |
Request delivery time estimate |
283.00€
|
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You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
You can also order by e-mail: info@biomol.com
Larger quantity required? Request bulk
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40... more
Product information "Anti-DD3"
This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. These enzymes catalyze the conversion of aldehydes and ketones to their corresponding alcohols by utilizing NADH and/or NADPH as cofactors. The enzymes display overlapping but distinct substrate specificity. This enzyme catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ), and the oxidation of 9alpha,11beta-PGF2 to PGD2. It may play an important role in the pathogenesis of allergic diseases such as asthma, and may also have a role in controlling cell growth and/or differentiation. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011], Protein function: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Acts as a NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain and regulates the metabolism of androgens, estrogens and progesterone (PubMed:10622721, PubMed:11165022, PubMed:7650035, PubMed:9415401, PubMed:9927279). Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH (PubMed:14672942, PubMed:11165022). Acts preferentially as a 17- ketosteroid reductase and has the highest catalytic efficiency of the AKR1C enzyme for the reduction of delta4-androstenedione to form testosterone (PubMed:20036328). Reduces prostaglandin (PG) D2 to 11beta-prostaglandin F2, progesterone to 20alpha-hydroxyprogesterone and estrone to 17beta-estradiol (PubMed:15047184, PubMed:20036328, PubMed:10622721, PubMed:11165022, PubMed:10998348, PubMed:19010934). Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol) (PubMed:10998348, PubMed:14672942, PubMed:11165022, PubMed:7650035, PubMed:9415401, PubMed:10557352). Also displays retinaldehyde reductase activity toward 9-cis-retinal (PubMed:21851338). [The UniProt Consortium] Recommended dilutions: Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications.. Cellular localization: Cytoplasm .
Keywords: | Anti-DD3, Anti-DDH1, Anti-DD-3, Anti-PGFS, Anti-AKR1C3, Anti-HA1753, Anti-17-beta-HSD 5, Anti-3-alpha-HSD type 2, Anti-Prostaglandin F synthase, Anti-3-alpha-HSD type II, brain, Anti-Dihydrodiol dehydrogenase 3, Anti-Dihydrodiol dehydrogenase type I, DD3 |
Supplier: | ELK Biotechnology |
Supplier-Nr: | ES7844 |
Properties
Application: | WB, ELISA |
Antibody Type: | Polyclonal |
Conjugate: | No |
Host: | Rabbit |
Species reactivity: | human, rat, mouse, |
Immunogen: | The antiserum was produced against synthesized peptide derived from human AKR1C3. AA range:191-240 |
MW: | 37 kD |
Format: | Antiserum |
Database Information
KEGG ID : | K04119 | Matching products |
UniProt ID : | P42330 | Matching products |
Gene ID | GeneID 8644 | Matching products |
Handling & Safety
Storage: | -20°C |
Shipping: | +4°C (International: +4°C) |
Caution
Our products are for laboratory research use only: Not for administration to humans!
Our products are for laboratory research use only: Not for administration to humans!
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