Akr1b8
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Official Full Name
aldo-keto reductase family 1, member B8
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Synonyms
FR-1; Fgrp; Fgfrp;
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Mouse | AKR1B8-1494M | Recombinant Mouse AKR1B8 Protein | Mammalian Cell | His | ||
Mouse | AKR1B8-437M | Recombinant Mouse AKR1B8 Protein, His (Fc)-Avi-tagged | HEK293 | His&Fc&Avi | ||
Mouse | AKR1B8-437M-B | Recombinant Mouse AKR1B8 Protein Pre-coupled Magnetic Beads | HEK293 |
- Involved Pathway
- Protein Function
- Interacting Protein
Akr1b8 involved in several pathways and played different roles in them. We selected most pathways Akr1b8 participated on our site, such as Pentose and glucuronate interconversions, Fructose and mannose metabolism, Galactose metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with Akr1b8 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Pentose and glucuronate interconversions | RPE;UGT1AB;Akr1b3;AKR1B1L;AKR1B1;DHDHL;UGT2A3;UGT1A7C;OXSR1 |
Fructose and mannose metabolism | TPI1;HKDC1;ALDOA;PFKFB4L;ALDOB;HK3;PFKL;TIGARA;MPI |
Galactose metabolism | GALM;B4GALT1;GANC;G6PCA.2;G6PCA.1;AKR1B1L;GALK1;PFKP;PFKMB |
Glycerolipid metabolism | PNPLA3;MOGAT1;LPL;AKR1A1;DGAT2;LPIN2;ALDH9A1B;CEL.1;LYCAT |
Metabolic pathways | POLR3G;GCNT4A;GPAA1;ACAT2;ALG13;INPP4A;GCNT4;SI;HSD17B12 |
Akr1b8 has several biochemical functions, for example, alditol:NADP+ 1-oxidoreductase activity, geranylgeranyl reductase activity, indanol dehydrogenase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by Akr1b8 itself. We selected most functions Akr1b8 had, and list some proteins which have the same functions with Akr1b8. You can find most of the proteins on our site.
Function | Related Protein |
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alditol:NADP+ 1-oxidoreductase activity | AKR1B1;AKR7A5;AKR7A2;AKR1C21;ADH4;AKR1C3;Akr1b3;AKR1B8;PRKRA |
geranylgeranyl reductase activity | AKR1C3;AKR1B8;AKR1B10 |
indanol dehydrogenase activity | AKR1B10;AKR1B8;AKR1C3 |
oxidoreductase activity | CYP8B3;CYP2C8;CYP2AD6;DHRS11A;HIBADHB;HSD17B6;KDM1B;YWHAE1;DIO3 |
retinal dehydrogenase activity | AKR1C6;ALDH1A3;ALDH1A1;AKR1B10;AKR1C4;ALDH8A1;AKR1B8;Aldh1a7;AKR1C3 |
Akr1b8 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with Akr1b8 here. Most of them are supplied by our site. Hope this information will be useful for your research of Akr1b8.
Ywhae
- Reviews
- Q&As
Customer Reviews (4)
Write a reviewIts purity and functionality ensure precise and reproducible results, enabling me to achieve my research objectives with confidence.
Great performance in ELISA.
The AKR1B8 protein is of exceptional quality and will undoubtedly meet my experimental needs with utmost reliability and accuracy.
By utilizing the AKR1B8 protein in my experiments, I can trust that I am working with a product of the highest caliber, backed by a company dedicated to delivering exceptional quality and support.
Q&As (15)
Ask a questionThere is limited research on AKR1B8 utilizing animal models. Some studies have investigated its expression and function in mice and rats, particularly in the context of liver cancer and diabetes-associated complications. Animal models can provide insights into the physiological and pathological roles of AKR1B8, but more research is needed to fully understand its significance.
Several compounds have been identified as potential inhibitors of AKR1B8, including nonsteroidal anti-inflammatory drugs (NSAIDs) such as indomethacin and diclofenac. However, more studies are needed to determine the specificity and efficacy of these compounds as AKR1B8 inhibitors. As for activators, there is limited information available regarding molecules that can enhance AKR1B8 activity.
Research on genetic variations in AKR1B8 is limited. However, some studies have reported single nucleotide polymorphisms (SNPs) in the AKR1B8 gene that may be associated with altered enzymatic activity. Further investigation is required to understand the implications of these genetic variations on human health.
Research has suggested that AKR1B8 may play a role in the pathogenesis of certain diseases. In particular, it has been implicated in hepatocellular carcinoma, as increased expression of AKR1B8 has been observed in liver cancer tissues. Additionally, AKR1B8 has been proposed as a potential therapeutic target for diabetic nephropathy due to its involvement in glucose metabolism and renal function.
AKR1B8 has been suggested to play a role in lipid metabolism, particularly in the liver. It is thought to participate in the detoxification of lipid-associated aldehydes, which can be generated during oxidative stress or lipid peroxidation. By reducing these aldehydes to their corresponding alcohols, AKR1B8 may contribute to maintaining cellular homeostasis and protecting against lipid-associated damage.
Yes, AKR1B8 has been shown to participate in the metabolism of certain drugs. For example, studies have found that it can catalyze the reduction of the anti-cancer drug mitomycin C, leading to the formation of its inactive metabolite. This suggests that AKR1B8 may influence the efficacy of mitomycin C treatment.
The specific substrates of AKR1B8 are not well characterized. However, being a member of the aldo-keto reductase superfamily, it is expected to have a broad substrate specificity for aldehydes and ketones. Further studies are needed to identify and characterize the exact substrates of AKR1B8.
The subcellular localization of AKR1B8 protein has not been extensively studied. However, it is predicted to be primarily localized within the cytoplasm due to its enzymatic function in metabolizing aldehydes and ketones. Further research is required to confirm its precise subcellular localization.
The therapeutic potential of AKR1B8 has not been extensively explored yet. However, as a member of the aldo-keto reductase superfamily, targeting AKR1B8 may hold promise in various pathological conditions involving aldehydes and ketones, such as oxidative stress, lipid peroxidation, and certain metabolic disorders. Further research is needed to investigate the specific roles of AKR1B8 in disease processes and to develop strategies for therapeutic intervention.
The regulation of AKR1B8 expression is not well understood. However, studies suggest that it may be influenced by various factors, including hormonal signals, environmental cues, and genetic alterations. Further research is needed to uncover the precise mechanisms that control AKR1B8 expression.
To the best of our knowledge, there have been no studies investigating the association between AKR1B8 polymorphisms and disease susceptibility so far. However, given the potential involvement of AKR1B8 in various metabolic processes and its expression in different tissues, it is plausible that genetic variability in AKR1B8 could influence disease risk or susceptibility. Further research is required to explore this aspect.
The exact physiological functions of AKR1B8 are not fully understood. However, as a member of the aldo-keto reductase superfamily, it likely contributes to cellular detoxification processes by metabolizing aldehydes and ketones. Additionally, its suggested involvement in lipid metabolism points towards a potential role in maintaining lipid homeostasis and protecting against lipid-associated damage. Further research is necessary to elucidate the specific physiological functions and regulatory mechanisms of AKR1B8.
AKR1B8 has been proposed as a potential therapeutic target for certain diseases, such as liver cancer and diabetic nephropathy. Inhibitors that specifically target AKR1B8 could potentially be developed to help combat these conditions. However, more research is needed to validate AKR1B8 as a therapeutic target and develop effective drug candidates.
To date, no specific inhibitors or activators of AKR1B8 have been reported in the literature. However, given its similarities to other members of the aldo-keto reductase superfamily, it is possible that some known inhibitors or activators of related enzymes could also exert effects on AKR1B8. Further research is needed to identify compounds that can selectively modulate AKR1B8 activity.
Limited information is available regarding the specific interactions or binding partners of AKR1B8. However, being a member of the aldo-keto reductase superfamily, it is likely to interact with various substrates, coenzymes, and other proteins within the cellular environment. Further studies are needed to elucidate the protein-protein interactions of AKR1B8.
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