aqp7p3
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Homo sapiens (Human) | RFL-1063HF | Recombinant Full Length Human Putative Aquaporin-7-Like Protein 3(Aqp7P3) Protein, Tag-Free | E.coli expression system | Tag-Free | Full Length (1-342) |
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Q&As (15)
Ask a questionThe specific alterations in AQP7P3 expression under various conditions or diseases have not been investigated due to the lack of research on this particular isoform. However, changes in the expression of aquaporins, including AQP7, have been observed in certain diseases and conditions, such as obesity, diabetes, kidney disorders, and cancer. Therefore, it is conceivable that alterations in AQP7P3 expression may occur under similar circumstances, but further research is needed to confirm this.
The specific alterations in AQP7P3 expression under various conditions or diseases have not been investigated due to the lack of research on this particular isoform. However, changes in the expression of aquaporins, including AQP7, have been observed in certain diseases and conditions, such as obesity, diabetes, kidney disorders, and cancer. Therefore, it is conceivable that alterations in AQP7P3 expression may occur under similar circumstances, but further research is needed to confirm this.
The specific role of AQP7P3 in physiological processes is not well understood. However, aquaporins, including AQP7, are known to contribute to various biological processes, such as water balance, osmoregulation, urine concentration, and metabolism. It is reasonable to speculate that AQP7P3 may play a similar role, but further research is needed to elucidate its involvement in specific physiological processes.
The specific role of AQP7P3 in physiological processes is not well understood. However, aquaporins, including AQP7, are known to contribute to various biological processes, such as water balance, osmoregulation, urine concentration, and metabolism. It is reasonable to speculate that AQP7P3 may play a similar role, but further research is needed to elucidate its involvement in specific physiological processes.
Currently, there is limited evidence suggesting a functional role for AQP7P3. The specific functions or transport properties of AQP7P3 have not been thoroughly investigated, and its physiological relevance is still unknown. However, based on the established roles of aquaporins in water and solute transport, it is reasonable to hypothesize that AQP7P3 may have similar functions. Further studies are required to determine the functional significance of AQP7P3.
Currently, there is limited evidence suggesting a functional role for AQP7P3. The specific functions or transport properties of AQP7P3 have not been thoroughly investigated, and its physiological relevance is still unknown. However, based on the established roles of aquaporins in water and solute transport, it is reasonable to hypothesize that AQP7P3 may have similar functions. Further studies are required to determine the functional significance of AQP7P3.
As of now, there is limited information available regarding genetic variants or mutations specifically associated with AQP7P3. However, genetic variations in other aquaporin genes, including AQP7, have been reported and associated with certain diseases or conditions. For example, mutations in AQP7 have been linked to impaired glucose metabolism and obesity. Further research is needed to determine if there are any specific genetic variants or mutations in the AQP7P3 gene and their potential implications.
As of now, there is limited information available regarding genetic variants or mutations specifically associated with AQP7P3. However, genetic variations in other aquaporin genes, including AQP7, have been reported and associated with certain diseases or conditions. For example, mutations in AQP7 have been linked to impaired glucose metabolism and obesity. Further research is needed to determine if there are any specific genetic variants or mutations in the AQP7P3 gene and their potential implications.
The tissue-specific or cell-type expression of AQP7P3 is not well characterized due to limited research on this specific isoform. However, other AQP7 isoforms have been found in various tissues, including adipose tissue, liver, kidney, urinary tract, and reproductive organs. It is plausible that AQP7P3 could be expressed in similar tissues, but more studies are needed to confirm this.
At present, there are no known clinical applications specifically associated with AQP7P3. However, aquaporins, including AQP7, have been studied as potential targets for therapeutic interventions in various diseases. Understanding the specific role of AQP7P3 and its potential involvement in cellular processes or diseases may contribute to future clinical applications. Nonetheless, further research is needed to explore the potential clinical implications of AQP7P3.
The protein-protein interactions or molecular interactions involving AQP7P3 have not been extensively investigated. However, aquaporins, including AQP7, can interact with other proteins, such as signaling molecules, transporters, and scaffolding proteins, to regulate their activity, cellular localization, or function. It is possible that AQP7P3 may exhibit similar interactions, but further research is required to determine its specific interactions.
As AQP7P3 is an isoform of AQP7, any genetic variations or mutations would likely be found in the AQP7 gene itself. However, it is important to note that the specific genetic variations and mutations associated with the AQP7P3 isoform, if any, have not been extensively studied or documented.
There is currently no direct evidence to suggest that AQP7P3 is associated with any specific diseases or conditions. Since it is an isoform of AQP7, it may have similar functions and potential associations as the main AQP7 protein. However, further research is needed to establish any specific links.
Currently, there are no known therapeutic implications specifically associated with AQP7P3. However, aquaporins, including AQP7, have been investigated as potential therapeutic targets in various diseases, such as kidney disorders, diabetes, obesity, and cancer. Understanding the functional significance of AQP7P3 may provide insights into its potential therapeutic relevance, although further research is required to explore this avenue.
Currently, there are no known therapeutic implications specifically associated with AQP7P3. However, aquaporins, including AQP7, have been investigated as potential therapeutic targets in various diseases, such as kidney disorders, diabetes, obesity, and cancer. Understanding the functional significance of AQP7P3 may provide insights into its potential therapeutic relevance, although further research is required to explore this avenue.
Customer Reviews (8)
Write a reviewIt has demonstrated exceptional effectiveness in WB experiments, showcasing its reliability and precision in detecting and quantifying specific targets.
Its stability and compatibility with electron microscopy techniques make it an ideal candidate for studying protein structures at high resolution.
Scientists who have employed AQP7P3 protein in their experiments have praised its outstanding performance and reliability.
The AQP7P3 protein comes highly recommended for its exceptional performance in various research applications.
Its exceptional purity and stability make it an ideal choice for a wide range of applications, ensuring reliable and reproducible results.
Its unique characteristics contribute to obtaining clear and detailed structural information, allowing researchers to gain insights into protein interactions and conformational changes.
Its versatility in various biological applications, coupled with its compatibility with diverse techniques, makes it a preferred reagent for researchers in the field.
Its high sensitivity enables the identification of low abundance targets, making it highly valuable in immunological research.
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