Recombinant Mouse AKR1B8 Protein, His (Fc)-Avi-tagged

• Cat.No.: AKR1B8-437M
• Product Overview: Recombinant Mouse AKR1B8 with His (Fc)-Avi tag was expressed and purified

Specification

• Source: HEK293
• Species: Mouse
• Tag: His (Fc)-Avi
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: ≥85% by SDS-PAGE
• Stability: Stable for at least 6 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
• Storage: For long term storage, aliquot and store at -20 to -80 centigrade. Avoid repeated freezing and thawing cycles.
• Storage Buffer: PBS buffer

Gene Information

• Gene Name: Akr1b8 aldo-keto reductase family 1, member B8 [ Mus musculus ]
• Official Symbol: AKR1B8
• Gene ID: 14187
• mRNA Refseq: NM_008012.1
• Protein Refseq: NP_032038.1
• UniProt ID: P45377

Reviews

07/02/2021

Its purity and functionality ensure precise and reproducible results, enabling me to achieve my research objectives with confidence.

11/12/2019

Great performance in ELISA.

10/02/2019

The AKR1B8 protein is of exceptional quality and will undoubtedly meet my experimental needs with utmost reliability and accuracy.

07/03/2019

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

Has AKR1B8 been studied in animal models?

There 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.

Are there any inhibitors or activators of AKR1B8?

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.

Are there any known genetic variations or mutations in AKR1B8?

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.

Are there any diseases associated with AKR1B8 protein?

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.

How is AKR1B8 protein involved in lipid metabolism?

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.

Is AKR1B8 protein involved in drug metabolism?

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.

Are there any known substrates of AKR1B8?

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.

How is AKR1B8 protein localized within the cell?

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.

Can AKR1B8 be a potential therapeutic target?

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.

How is the expression of AKR1B8 regulated?

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.

Is there any association between AKR1B8 polymorphisms and disease susceptibility?

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.

What are the potential physiological functions of AKR1B8?

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.

Does AKR1B8 have any potential as a therapeutic target?

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.

Are there any inhibitors or activators of AKR1B8 identified?

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.

Are there any known interactions or binding partners of AKR1B8 protein?

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.