AQP8
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Official Full Name
aquaporin 8
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Overview
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to;the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. -
Synonyms
AQP8; aquaporin 8; aquaporin-8; AQP-8;
- Recombinant Proteins
- Cell & Tissue Lysates
- Antibody
- Protein Pre-coupled Magnetic Beads
- Homo sapiens (Human)
- Human
- Milnesium tardigradum (Water bear) (Tardigrade)
- Mouse
- Mus musculus (Mouse)
- Notomys alexis (Spinifex hopping mouse)
- Rat
- Rattus norvegicus (Rat)
- E.coli
- E.coli expression system
- E.Coli or Yeast
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- His|GST
- N/A
- Tag
- Free
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Human | AQP8-658H | Recombinant Human AQP8 | Mammalian Cell | His | ||
Human | AQP8-736H | Recombinant Human AQP8 protein, GST-tagged | Wheat Germ | GST | ||
Human | AQP8-8246H | Recombinant Human AQP8 protein, His & GST-tagged | E.coli | His/GST | Lys129~Trp228 (Accession # O94778) | |
Human | AQP8-34HCL | Recombinant Human AQP8 lysate | HEK293 | N/A | ||
Human | AQP8-1126HF | Recombinant Full Length Human AQP8 Protein, GST-tagged | In Vitro Cell Free System | GST | 255 amino acids | |
Human | AQP8-26532TH | Recombinant Human AQP8 | Wheat Germ | N/A | 255 amino acids | |
Human | AQP8-2490H | Recombinant Human AQP8 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Human | AQP8-27HF | Recombinant Full Length Human AQP8 Protein | In Vitro Cell Free System | 255 amino acids | ||
Human | AQP8-2490H-B | Recombinant Human AQP8 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Mouse | AQP8-1827M | Recombinant Mouse AQP8 Protein | Mammalian Cell | His | ||
Mouse | AQP8-653M-B | Recombinant Mouse AQP8 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Mouse | AQP8-653M | Recombinant Mouse AQP8 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
Rat | Aqp8-3605R | Recombinant Rat Aqp8, His-tagged | E.Coli or Yeast | His | 263 | |
Homo sapiens (Human) | RFL-34772HF | Recombinant Full Length Human Aquaporin-8(Aqp8) Protein, His-Tagged | E.coli expression system | His | Full Length (1-261) | |
Milnesium tardigradum (Water bear) (Tardigrade) | RFL17906MF | Recombinant Full Length Milnesium Tardigradum Aquaporin-8(Aqp8) Protein, Tag-Free | E.coli expression system | Tag-Free | Full Length (1-342) | |
Mus musculus (Mouse) | RFL-20804MF | Recombinant Full Length Mouse Aquaporin-8(Aqp8) Protein, His-Tagged | E.coli expression system | His | Full Length (1-261) | |
Notomys alexis (Spinifex hopping mouse) | RFL7106NF | Recombinant Full Length Notomys Alexis Aquaporin-8(Aqp8) Protein, His-Tagged | E.coli expression system | His | Full Length (1-261) | |
Rattus norvegicus (Rat) | RFL-34606RF | Recombinant Full Length Rat Aquaporin-8(Aqp8) Protein, His-Tagged | E.coli expression system | His | Full Length (1-263) |
- Involved Pathway
- Protein Function
- Interacting Protein
- AQP8 Related Articles
AQP8 involved in several pathways and played different roles in them. We selected most pathways AQP8 participated on our site, such as Bile secretion, which may be useful for your reference. Also, other proteins which involved in the same pathway with AQP8 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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Bile secretion | Car2;SLC9A1;ADCY9;Adcy4;SCARB1;AQP4;ATP1A2;SLC22A8;ATP1A4 |
AQP8 has several biochemical functions, for example, glycerol channel activity, water channel activity. Some of the functions are cooperated with other proteins, some of the functions could acted by AQP8 itself. We selected most functions AQP8 had, and list some proteins which have the same functions with AQP8. You can find most of the proteins on our site.
Function | Related Protein |
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glycerol channel activity | AQP7;AQP8;AQP8B;AQP10;AQP3B;MIPB;AQP8A.1;AQP1A.2;AQP2 |
water channel activity | AQP3;AQP2;AQP9;AQP3B;AQP3A;AQP8;AQP1A.2;AQP8B;AQP8A.1 |
AQP8 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 AQP8 here. Most of them are supplied by our site. Hope this information will be useful for your research of AQP8.
- Q&As
- Reviews
Q&As (26)
Ask a questionCurrently, there are no approved drugs that directly target AQP8. However, researchers are actively studying and exploring the potential of AQP8 as a therapeutic target. Some studies have investigated the use of compounds that modulate AQP8 activity as potential treatments for certain liver diseases.
There is limited evidence suggesting that AQP8 may play a role in drug transport and drug resistance. Some studies have proposed that AQP8 could potentially affect the uptake or efflux of certain drugs, impacting their efficacy or resistance. However, further research is needed to fully understand the implications of AQP8 in drug pharmacokinetics and resistance mechanisms.
There is limited evidence suggesting that AQP8 may play a role in drug transport and drug resistance. Some studies have proposed that AQP8 could potentially affect the uptake or efflux of certain drugs, impacting their efficacy or resistance. However, further research is needed to fully understand the implications of AQP8 in drug pharmacokinetics and resistance mechanisms.
While AQP8 shows promise as a potential biomarker for certain diseases, more research is needed to establish its clinical utility. Studies have suggested that altered AQP8 expression may be associated with liver diseases, digestive disorders, and some cancers. However, further investigation is required to determine its diagnostic or prognostic value in clinical settings.
While AQP8 shows promise as a potential biomarker for certain diseases, more research is needed to establish its clinical utility. Studies have suggested that altered AQP8 expression may be associated with liver diseases, digestive disorders, and some cancers. However, further investigation is required to determine its diagnostic or prognostic value in clinical settings.
There is evidence suggesting that alterations in AQP8 expression or function may be implicated in cancer development. Studies have reported changes in AQP8 levels in various types of tumors, including hepatocellular carcinoma, colon cancer, and pancreatic cancer. Further research is being conducted to unravel the precise role of AQP8 in tumorigenesis and its potential as a therapeutic target.
Yes, AQP8 has been found to be expressed in the central nervous system, including regions such as the brain and spinal cord. It is involved in the regulation of water movement across brain cells and plays a role in maintaining brain homeostasis.
Yes, AQP8 has been found to be expressed in the central nervous system, including regions such as the brain and spinal cord. It is involved in the regulation of water movement across brain cells and plays a role in maintaining brain homeostasis.
AQP8 dysfunction has been associated with various health conditions. For example, in the liver, altered AQP8 expression has been linked to liver cirrhosis, cholestasis, and non-alcoholic fatty liver disease. In the digestive tract, changes in AQP8 expression have been observed in inflammatory bowel disease and diarrhea. Understanding the role of AQP8 in these conditions may provide insights for potential therapeutic interventions.
While there are no specific inhibitors or activators of AQP8 currently approved for clinical use, researchers are actively studying compounds that could modulate its activity. These studies aim to identify potential therapeutic targets for conditions related to AQP8 dysregulation.
The regulation of AQP8 expression in the gastrointestinal tract is complex and not fully understood. Multiple factors, such as hormones, cytokines, and dietary components, may influence its expression. For example, bile acids have been shown to upregulate AQP8 expression in the liver and small intestine.
The regulation of AQP8 expression in the gastrointestinal tract is complex and not fully understood. Multiple factors, such as hormones, cytokines, and dietary components, may influence its expression. For example, bile acids have been shown to upregulate AQP8 expression in the liver and small intestine.
AQP8 is being explored as a potential therapeutic target for various diseases. Researchers are investigating the development of drugs that can modulate AQP8 activity, particularly in liver diseases and certain cancers. Inhibition or activation of AQP8 could potentially be used to manage fluid balance disorders, liver diseases, and other conditions.
AQP8 is being explored as a potential therapeutic target for various diseases. Researchers are investigating the development of drugs that can modulate AQP8 activity, particularly in liver diseases and certain cancers. Inhibition or activation of AQP8 could potentially be used to manage fluid balance disorders, liver diseases, and other conditions.
Some studies have suggested a potential link between AQP8 expression and obesity. Alterations in AQP8 levels have been reported in adipose tissue of obese individuals. Further research is needed to ascertain the precise role and mechanisms through which AQP8 may contribute to obesity and related metabolic disorders.
Some studies have suggested a potential link between AQP8 expression and obesity. Alterations in AQP8 levels have been reported in adipose tissue of obese individuals. Further research is needed to ascertain the precise role and mechanisms through which AQP8 may contribute to obesity and related metabolic disorders.
While more research is needed, studies have implicated AQP8 dysfunction in various diseases and conditions. For example, altered expression or activity of AQP8 has been linked to liver diseases, such as non-alcoholic fatty liver disease (NAFLD) and liver fibrosis. Changes in AQP8 expression have also been observed in digestive disorders, including inflammatory bowel disease (IBD) and ulcerative colitis.
While more research is needed, studies have implicated AQP8 dysfunction in various diseases and conditions. For example, altered expression or activity of AQP8 has been linked to liver diseases, such as non-alcoholic fatty liver disease (NAFLD) and liver fibrosis. Changes in AQP8 expression have also been observed in digestive disorders, including inflammatory bowel disease (IBD) and ulcerative colitis.
Yes, besides its role in water transport, AQP8 has been implicated in several other physiological processes. For example, it is involved in the transport of glycerol, which is important for energy metabolism. AQP8 has also been shown to facilitate hydrogen peroxide transport, potentially impacting oxidative stress responses within the cell.
Yes, AQP8 is expressed in the kidney and has been implicated in water reabsorption in the renal tubules. It plays a role in maintaining water balance and urinary concentration. AQP8 function in the kidney is essential for proper kidney function and fluid homeostasis.
Yes, AQP8 is expressed in the kidney and has been implicated in water reabsorption in the renal tubules. It plays a role in maintaining water balance and urinary concentration. AQP8 function in the kidney is essential for proper kidney function and fluid homeostasis.
Although AQP8 is primarily known for its role as a water channel, studies have suggested its involvement in the transport of other small solutes, such as glycerol and hydrogen peroxide. However, more research is needed to fully understand these additional functions.
Yes, ongoing research continues to explore the role of AQP8 in various physiological and pathological contexts. Scientists are investigating its involvement in liver diseases, digestive disorders, and metabolic regulation, among other areas of interest. These studies aim to deepen our understanding of AQP8's functions and potential therapeutic applications.
Yes, animal models, such as mice, have been used to study AQP8 function and regulation. Knockout mouse models lacking the AQP8 gene have been developed to investigate its physiological roles. These models have provided insights into the impact of AQP8 deficiency on various organs and systems.
Yes, animal models, such as mice, have been used to study AQP8 function and regulation. Knockout mouse models lacking the AQP8 gene have been developed to investigate its physiological roles. These models have provided insights into the impact of AQP8 deficiency on various organs and systems.
Yes, certain genetic mutations in the AQP8 gene have been identified and associated with specific disorders. For instance, a mutation in AQP8 has been linked to primary male infertility, affecting sperm motility and function. These genetic abnormalities contribute to our understanding of AQP8's importance in reproductive processes.
Customer Reviews (8)
Write a reviewThe reliable performance of the AQP8 protein in ELISA and its compatibility with protein electron microscopy structure analysis make it an excellent choice for a wide range of research studies.
AQP8 protein is highly recommended for scientific research applications, especially in ELISA assays and protein electron microscopy structure analysis.
AQP8 protein has proven to be instrumental in protein electron microscopy structure analysis.
With AQP8 protein, researchers can visualize protein complexes and their interactions with remarkable clarity, unraveling important insights into their functional mechanisms.
The AQP8 protein comes highly recommended for its excellent performance in various research applications.
Researchers can confidently rely on its capabilities to generate precise and significant results, enhancing the understanding of protein function and dynamics.
Its reliable and accurate performance ensures dependable results, contributing to the advancement of scientific knowledge in various fields of study.
This protein demonstrates exceptional performance in ELISA, delivering accurate and reliable results in the detection and quantification of specific antigens.
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