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Anti-AKR1D1 Antibody Picoband®

Boster Bio Anti-AKR1D1 Antibody Picoband® catalog # A05278-2. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.

Product Specifications

Background

Human delta (4) -3-oxosteroid 5-beta-reductase (steroid 5-beta-reductase) catalyzes 5-beta-reduction of bile acid intermediates and steroid hormones carrying a delta (4) -3-one structure. This gene is mapped to 7q33. The enzyme encoded by this gene is responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones carrying a delta (4) -3-one structure. Deficiency of this enzyme may contribute to hepatic dysfunction. Three transcript variants encoding different isoforms have been found for this gene. Other variants may be present, but their full-length natures have not been determined yet.

Synonyms

Aldo-keto reductase family 1 member D1; 3-oxo-5-beta-steroid 4-dehydrogenase; Delta (4) -3-ketosteroid 5-beta-reductase; Delta (4) -3-oxosteroid 5-beta-reductase; AKR1D1; SRD5B1

Gene Name

AKR1D1

Gene ID

6718

UniProt

P51857

Host

Rabbit

Reactivity

Human, Mouse, Rat

Cross Reactivity

No cross-reactivity with other proteins.

Immunogen

A synthetic peptide corresponding to a sequence in the middle region of human SMAD5, which shares 95.5% amino acid (aa) sequence identity with both mouse and rat SMAD5.

Clonality

Polyclonal

Tissue Specificity

Highly expressed in liver. Expressed in testis and weakly in colon.

Applications

Flow Cytometry, IF, IHC, ICC, WB

Field of Research

Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction, Cancer, Cardiovascular, Lipid and Lipoprotein Metabolism, Cancer Metabolism, Lipid Metabolism, Metabolic Signaling Pathway, Metabolism of Lipids and Lipoproteins, Cholesterol Metabolism, Lipids/Lipoproteins

Purification

Immunogen affinity purified.

Concentration

Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.

Form

Lyophilized

Reconstitution

Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

Function

Catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of bile acid intermediates and steroid hormones carrying a delta4-3-one structure to yield an A/B cis-ring junction. This cis-configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. Capable of reducing a broad range of delta-4-3-ketosteroids from C18 (such as, 17beta-hydroxyestr-4-en-3-one) to C27 (such as, 7alpha-hydroxycholest-4-en-3-one) .

References & Citations

1. Charbonneau, A., Luu-The, V. Assignment of steroid 5-beta-reductase (SRD5B1) and its pseudogene (SRD5BP1) to human chromosome bands 7q32-q33 and 1q23-q25, respectively, by in situ hybridization. Cytogenet. Cell Genet. 84: 105-106, 1999. 2. Charbonneau, A., The, V.-L. Genomic organization of a human 5-beta-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim. Biophys. Acta 1517: 228-235, 2001. 3. Clayton, P. T., Mills, K. A., Johnson, A. W., Barabino, A., Marazzi, M. G. Delta 4-3-oxosteroid 5 beta-reductase deficiency: failure of ursodeoxycholic acid treatment and response to chenodeoxycholic acid plus cholic acid. Gut 38: 623-628, 1996.

Storage Conditions

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Calculated Molecular Weight

39411 MW

Observed Molecular Weight

37 kDa

Specificity

No cross reactivity with other proteins.

Applications Notes

6

Gene Name Synonym

Aldo-keto reductase family 1 member D1

Subcellular Location

Cytoplasm.

Protein Name

Zinc finger protein Helios

Isotype

Rabbit IgG

Contents

243

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