Recombinant Human AKR1C1 cell lysate
- Gene Information
- Related Products
|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 reaction of progesterone to the inactive form 20-alpha-hydroxy-progesterone. This gene shares high sequence identity with three other gene members and is clustered with those three genes at chromosome 10p15-p14.
|Storage Buffer :
|1X Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2-mercaptoethanol, 0.01% Bromophenol blue)
|Gene Name :
|AKR1C1 aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase) [ Homo sapiens ]
|Official Symbol :
|AKR1C1; aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase); DDH1; aldo-keto reductase family 1 member C1; DD1; DDH; HAKRC; MBAB; aldo-keto reductase C; indanol dehydrogenase; dihydrodiol dehydrogenase 1; dihydrodiol dehydrogenase 1/2; hepatic dihydrodiol dehydrogenase; chlordecone reductase homolog HAKRC; 20 alpha-hydroxysteroid dehydrogenase; 20-alpha-hydroxysteroid dehydrogenase; dihydrodiol dehydrogenase isoform DD1; type II 3-alpha-hydroxysteroid dehydrogenase; high-affinity hepatic bile acid-binding protein; trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; C9; H-37; HBAB; DD1/DD2; 2-ALPHA-HSD; 20-ALPHA-HSD; MGC8954;
|Gene ID :
|mRNA Refseq :
|Protein Refseq :
|UniProt ID :
|Chromosome Location :
|Metabolism of xenobiotics by cytochrome P450, organism-specific biosystem; Metabolism of xenobiotics by cytochrome P450, conserved biosystem; Steroid hormone biosynthesis, organism-specific biosystem; Steroid hormone biosynthesis, conserved biosystem;
|17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity; alditol:NADP+ 1-oxidoreductase activity; aldo-keto reductase (NADP) activity; androsterone dehydrogenase (B-specific) activity; bile acid binding; carboxylic acid binding; indanol dehydrogenase activity; ketosteroid monooxygenase activity; oxidoreductase activity; oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor; phenanthrene 9,10-monooxygenase activity; trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity;
|◆ Recombinant Protein
|Recombinant Cynomolgus Monkey AKR1C1 Protein, His (Fc)-Avi-tagged
|Recombinant Rhesus Macaque AKR1C1 Protein, His (Fc)-Avi-tagged
|Recombinant Human AKR1C1 Protein, GST-tagged
|Recombinant Rhesus monkey AKR1C1 Protein, His-tagged
|Recombinant Cynomolgus AKR1C1 Protein, His-tagged
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Q&As (15)Ask a question
Mutations or dysregulation of AKR1C1 have been implicated in several diseases. For example, deficiency in AKR1C1 activity can lead to cortisone reductase deficiency type 1, a rare inherited disorder characterized by cortisol deficiency and excessive androgen production. AKR1C1 dysregulation has also been associated with certain types of cancer, as mentioned earlier. Furthermore, alterations in AKR1C1 expression or activity have been observed in conditions such as endometriosis, prostate hyperplasia, and obesity, suggesting potential roles in these diseases as well.
In addition to its role in steroid hormone metabolism, AKR1C1 likely has other physiological functions. It may be involved in maintaining the redox balance within cells by catalyzing the reduction of aldehydes and ketones. Additionally, AKR1C1 has been suggested to play a role in inflammation, oxidative stress, and tissue development, although further investigation is needed to fully understand these functions.
Yes, targeting AKR1C1 has been explored as a therapeutic strategy in cancer treatment. As mentioned earlier, AKR1C1 inhibitors are being developed to disrupt the balance of steroid hormones in the tumor microenvironment and potentially inhibit tumor growth. In addition, AKR1C1 inhibitors may sensitize cancer cells to hormone therapy or other anticancer drugs. Further research is needed to determine the efficacy and safety of these therapeutic strategies, but they represent a promising approach in cancer therapy.
Yes, there are several natural and synthetic compounds that have been shown to modulate AKR1C1 activity. For example, some flavonoids and polyphenols found in fruits and vegetables have been identified as AKR1C1 inhibitors. Certain drugs, such as nonsteroidal anti-inflammatory drugs (NSAIDs) and statins, can also affect AKR1C1 activity. In addition, endogenous compounds like retinoic acid and bile acids have been shown to regulate AKR1C1 expression and activity. The identification and characterization of these compounds provide potential avenues for therapeutic interventions targeting AKR1C1.
AKR1C1 has been investigated as a potential biomarker in various diseases. Its altered expression or activity in certain cancers, such as breast and prostate cancer, has shown promise as a diagnostic or prognostic marker. However, further research is needed to validate its utility as a biomarker and determine its specificity and sensitivity in different disease contexts.
Yes, AKR1C1 has been found to interact with other proteins and participate in various signaling pathways. For example, AKR1C1 has been shown to interact with nuclear receptors, such as the progesterone receptor and androgen receptor, influencing their transcriptional activity. AKR1C1 can also interact with enzymes involved in steroid hormone metabolism and drug metabolism, forming metabolic networks within cells. Understanding these interactions can provide insights into the complex roles of AKR1C1 in cellular processes.
Yes, several inhibitors and activators of AKR1C1 have been identified. Some inhibitors include flufenamic acid, indomethacin, and medroxyprogesterone acetate. These compounds can selectively bind to AKR1C1 and inhibit its enzymatic activity. On the other hand, some activators, such as NADPH and ATP, are required cofactors for the enzymatic function of AKR1C1.
Yes, AKR1C1 continues to be an active area of research. Scientists are investigating its role in various diseases, including cancer, and exploring its potential as a therapeutic target or biomarker. The structural and functional characterization of AKR1C1 is also an important focus, as it helps in understanding its enzymatic mechanisms and potential for drug development. Additionally, the identification of genetic polymorphisms and regulatory pathways associated with AKR1C1 is an ongoing area of investigation.
AKR1C1 inhibitors have been explored for their potential therapeutic applications, primarily in the context of cancer treatment. By inhibiting AKR1C1, it is hoped that the balance of steroid hormones within the tumor microenvironment can be disrupted, leading to decreased tumor growth or increased sensitivity to hormone therapy. The use of AKR1C1 inhibitors in combination with other therapeutic agents is also being investigated. However, it is important to note that the development of AKR1C1 inhibitors for clinical use is still in the early stages.
AKR1C1 is a key enzyme involved in the metabolism of steroid hormones. It primarily catalyzes the reduction of 5α-dihydrosteroids and 5β-dihydrosteroids. For example, AKR1C1 converts testosterone to dihydrotestosterone (DHT), a potent androgen. It also participates in the metabolism of progesterone, cortisone, and other steroid hormones. The activity of AKR1C1 in steroid hormone metabolism helps maintain the balance of these hormones and is crucial for normal physiological functions.
AKR1C1 has been considered as a potential therapeutic target in certain diseases, including cancer. Inhibitors of AKR1C1 have been explored for their potential anticancer properties by targeting steroid hormone metabolism or reversing drug resistance. However, further research is needed to fully understand the therapeutic potential and safety of targeting AKR1C1.
AKR1C1 expression and activity can be regulated at multiple levels. Transcriptional regulation is one mechanism, where factors such as hormones, cytokines, and growth factors can influence AKR1C1 gene expression. Epigenetic modifications, such as DNA methylation and histone modifications, can also affect AKR1C1 expression. Additionally, post-transcriptional regulation, including alternative splicing, microRNA-mediated regulation, and protein stabilization or degradation, can modulate AKR1C1 activity.
Yes, several genetic polymorphisms have been identified in the AKR1C1 gene. These polymorphisms can lead to variations in AKR1C1 expression or activity, which may contribute to interindividual differences in steroid hormone metabolism and response to drugs. The functional implications of these polymorphisms are still being studied.
Yes, there are known functional variants of AKR1C1 that have been identified through genetic studies. For example, certain single nucleotide polymorphisms (SNPs) in the AKR1C1 gene have been associated with altered enzyme activity or expression. These functional variants can impact the metabolism of steroid hormones and other substrates of AKR1C1, potentially influencing disease risk or drug response. Understanding the functional implications of these variants is important in personalized medicine and optimizing treatment strategies.
Yes, AKR1C1 polymorphisms have been associated with inter-individual differences in drug response and metabolism. These genetic variations can affect the function and activity of AKR1C1, leading to altered drug metabolism and response. For example, certain AKR1C1 polymorphisms have been linked to variations in the metabolism of drugs such as tamoxifen and nonsteroidal anti-inflammatory drugs (NSAIDs). Understanding the impact of AKR1C1 polymorphisms on drug metabolism can help in optimizing drug therapies and improving patient outcomes.
Customer Reviews (4)Write a review
Its high purity and integrity provide the necessary assurance for consistent and reliable results, enabling me to achieve precise and meaningful outcomes in my research.
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By incorporating the AKR1C1 protein into my experiments, I am confident that I am utilizing a product that meets the highest standards of quality and performance.
The AKR1C1 protein demonstrates exceptional quality, making it an ideal candidate to fulfill my experimental requirements.
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