Recombinant Full Length Milnesium Tardigradum Aquaporin-1(Aqp1) Protein, Tag-Free
Cat.No. : | RFL29573MF |
Product Overview : | Recombinant Full Length Milnesium tardigradum Aquaporin-1(AQP1) Protein (G5CTF8) (1-333aa) was expressed in E. coli. |
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Source : | E.coli expression system |
Species : | Milnesium tardigradum (Water bear) (Tardigrade) |
Tag : | Tag-Free |
Form : | Lyophilized powder |
Protein Length : | Full Length (1-333) |
AA Sequence : | MQKMSEKPLYRAAENPTRNADRRAG RFEEEELISKTGRHPDMVIQFQDDA DDQHTSHYEGNWRHYFHKKLHIKNR LIRDWLSESLAMFLFMSLLLGGAAT AHFTGKQDDPMLTAVFHGFSAVFGI YVGAGVSGGIINPALTFAVALLGRV SWRKCLVLVSAQYFGSFIASAVVYL IYYESLQNYAKTADDNGEFLQKTAG IWSTFPKPYLSMTGAIFNQIFCTML LSIGFLSISDHKNFRPTKGLFPFAV GLLIMTVFLAFSYSAGAAMNPARDL SPRLWSLIIGYGNEVFSHNDYKWFW IPWLFPYVGALFGAVMYQIFVGVHW PDKQSTKR Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
Purity : | Greater than 90% as determined by SDS-PAGE. |
Notes : | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Storage : | Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. |
Storage Buffer : | Tris/PBS-based buffer, 6% Trehalose, pH 8.0 |
Reconstitution : | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
Gene Name : | AQP1 |
Synonyms : | AQP1Aquaporin-1; AQP-1 |
UniProt ID : | G5CTF8 |
Gene Name : | AQP1 |
Synonyms : | AQP1Aquaporin-1; AQP-1 |
UniProt ID : | G5CTF8 |
Products Types
◆ Recombinant Protein | ||
AQP1-391R | Recombinant Rat AQP1 Protein, His (Fc)-Avi-tagged | +Inquiry |
AQP1-646M | Recombinant Mouse AQP1 Protein, His (Fc)-Avi-tagged | +Inquiry |
AQP1-367H | Recombinant Human AQP1 Protein, His (Fc)-Avi-tagged | +Inquiry |
Aqp1-233R | Recombinant Rat Aqp1 Protein, His&GST-tagged | +Inquiry |
Aqp1-1670M | Recombinant Mouse Aqp1 Protein, Myc/DDK-tagged | +Inquiry |
◆ Lysates | ||
AQP1-8770HCL | Recombinant Human AQP1 293 Cell Lysate | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (29)
Ask a questionYes, AQP1 dysfunction has been associated with various diseases and conditions. For example, mutations in the AQP1 gene have been linked to hereditary recessive foveal hypoplasia, which is characterized by impaired water transport in the retina. Additionally, AQP1 has been implicated in the development and progression of conditions like acute respiratory distress syndrome (ARDS), cerebral edema, and kidney disorders.
Currently, there are no FDA-approved drugs or specific inhibitors targeting AQP1. However, there is ongoing research towards the development of AQP1 modulators and blockers that could potentially be used for therapeutic purposes.
Yes, AQP1 has been implicated in cancer progression and metastasis in certain types of cancer. It has been shown to be upregulated in various cancer cells, including colorectal, lung, and breast cancer cells. AQP1 has been suggested to promote tumor angiogenesis, invasion, and migration by facilitating water and ion transport across cell membranes. However, the exact mechanisms by which AQP1 contributes to cancer progression are still being studied.
Yes, apart from its role in water transport, AQP1 has been implicated in other physiological processes. For example, it has been suggested to play a role in cell migration and angiogenesis, as well as in the regulation of endothelial cell function and blood vessel permeability.
Yes, mutations in the AQP1 gene can lead to various diseases or conditions. One example is the deficiency of AQP1 in red blood cells, which can result in hereditary stomatocytosis, a rare condition characterized by abnormal red blood cell shape and reduced cell flexibility. Other AQP1 mutations have been associated with hydrocephalus, a condition characterized by the accumulation of cerebrospinal fluid in the brain.
Yes, AQP1 is expressed in the respiratory system, specifically in the alveolar cells of the lungs. It helps in the transport of water across the alveolar epithelium, contributing to the proper humidification of inhaled air and the maintenance of lung function.
The role of AQP1 in various diseases has sparked interest in targeting the protein for therapeutic purposes. Modulating AQP1 expression or activity may hold promise for treating conditions involving fluid imbalances, such as renal disorders, edema, and certain cancers. However, further research is needed to develop specific pharmacological approaches targeting AQP1.
Yes, AQP1 expression and activity can be regulated by various factors. For example, water deprivation, osmotic gradients, hormone signaling, and changes in intracellular calcium levels can all influence AQP1 expression and cellular localization, thereby modulating its water transport capacity.
Several factors can downregulate the expression or activity of AQP1. For instance, inflammatory cytokines such as tumor necrosis factor-alpha (TNF-alpha) can decrease AQP1 expression in various tissues. Additionally, certain drugs or chemical agents, such as mercury and cadmium, have been shown to inhibit AQP1 activity.
Yes, certain polymorphisms or variations in the AQP1 gene have been identified and associated with specific diseases or conditions. For example, a single nucleotide polymorphism (SNP) known as AQP1-732C > T has been linked to increased risk of primary open-angle glaucoma. Other AQP1 polymorphisms have been studied in relation to conditions like diabetic retinopathy and essential hypertension, although more research is still needed to establish clear associations.
Yes, AQP1 plays a crucial role in the regulation of fluid balance in the body. It is involved in the reabsorption of water from various body fluids, including urine in the kidneys and respiratory secretions in the lungs. By facilitating water transport across cell membranes, AQP1 helps maintain proper hydration levels and fluid homeostasis.
Yes, AQP1 plays a vital role in maintaining fluid balance in the eye. It is expressed in the ciliary body and epithelium of the lens, where it facilitates the movement of water, ions, and nutrients, helping to maintain proper intraocular pressure and transparency of the lens.
Several inhibitors of AQP1 have been identified and tested in preclinical studies. These include small molecule inhibitors like mercury-based compounds (such as HgCl2) and arylsulfonamide derivatives. These inhibitors can block the water transport activity of AQP1 and have been explored for their potential therapeutic use, particularly in cancer. However, further studies are needed to determine their efficacy and safety in clinical settings. There are currently no known activators of AQP1, as its activity is mainly regulated by other factors like hormonal and cellular signaling pathways.
Yes, AQP1 plays a role in the regulation of cell volume. By facilitating the movement of water across cell membranes, AQP1 helps maintain cell hydration and prevents excessive swelling or shrinkage of cells in response to changes in osmolarity or osmotic stress.
Yes, AQP1 has been detected in certain regions of the central nervous system (CNS), including the choroid plexus and ependymal cells. It is involved in the regulation of cerebrospinal fluid (CSF) formation and circulation. AQP1 allows for the movement of water across the blood-brain barrier, aiding in the exchange of water and solutes between the blood and the CNS.
The role of AQP1 in various diseases and its involvement in water transport make it an attractive target for therapeutic purposes. Several research studies have explored the use of AQP1 inhibitors, antibodies, or gene therapy approaches to modulate its function and potentially treat conditions such as cancer, brain edema, and certain kidney disorders. However, further studies are needed to determine the efficacy and safety of such therapeutic approaches.
While AQP1 primarily transports water, it can also facilitate the movement of small solutes such as urea, glycerol, and certain gases (e.g., carbon dioxide and nitric oxide). These molecules can pass through the narrow pore of AQP1 by a process called "paracellular permeability."
Yes, mutations or alterations in AQP1 have been implicated in several diseases. For instance, mutations in the AQP1 gene can lead to abnormalities in urinary concentration and renal function, resulting in conditions like nephrogenic diabetes insipidus. AQP1 dysregulation has also been implicated in diseases such as lung edema, brain edema, and certain types of cancer.
AQP1 can interact with other proteins or molecules to modulate its function. For example, AQP1 has been reported to interact with caveolin-1, an integral component of caveolae, to regulate its cellular localization and trafficking. Additionally, phosphorylation events mediated by protein kinases can modulate AQP1 activity and cellular responses in various tissues.
Yes, targeting AQP1 has shown potential therapeutic implications in various diseases. For instance, in cancer, inhibiting AQP1 has been explored as a strategy to inhibit tumor angiogenesis and metastasis. In kidney disorders, modulating AQP1 expression or activity may help regulate fluid balance and alleviate symptoms associated with disorders like polycystic kidney disease or nephrogenic diabetes insipidus. Additionally, targeting AQP1 in conditions like cerebral edema and acute respiratory distress syndrome (ARDS) may help reduce fluid accumulation and improve patient outcomes.
Yes, AQP1 expression can be regulated by hormones. For instance, in the kidney, the antidiuretic hormone vasopressin (ADH) can stimulate the translocation and insertion of AQP1 into the cell membrane, increasing water reabsorption. Similarly, hormonal regulation of AQP1 expression has been observed in other tissues, such as the respiratory epithelium.
Yes, besides AQP1, there are several other isoforms of aquaporin proteins. Some of the well-known isoforms include AQP2, AQP3, AQP4, AQP5, AQP7, and AQP9. Each isoform has a slightly different tissue distribution and function, allowing them to play unique roles in water and solute transport in various organs and tissues.
AQP1 expression or dysregulation has been observed in various diseases, making it a potential biomarker. For example, increased AQP1 expression has been associated with certain types of cancer, including lung, breast, and pancreatic cancers. Additionally, altered expression of AQP1 has been observed in conditions like glaucoma, brain edema, and kidney disorders.
Yes, AQP1 is involved in the transport of water across the placenta during pregnancy. It is expressed in the maternal and fetal vascular endothelial cells of the placenta, facilitating the movement of water and solutes between the mother and fetus.
AQP1 is not extensively expressed in the gastrointestinal system. However, it has been detected in specific regions, such as the gastric parietal cells and the secretory cells of the salivary glands. In these locations, AQP1 is involved in the regulation of fluid secretion and saliva production.
No, AQP1 is not involved in the direct transport of gases such as oxygen (O2) and carbon dioxide (CO2). Its main function is to facilitate the movement of water molecules across cell membranes. However, the presence of AQP1 in certain tissues, such as the lungs and the red blood cells, indirectly contributes to the exchange and regulation of gases by maintaining the proper hydration and function of these tissues.
While AQP1 primarily facilitates the movement of water molecules across cell membranes, it has been shown to have some limited permeability to small solutes, such as glycerol and urea. However, its transport of solutes is far less efficient compared to its water transport capabilities.
AQP1 is synthesized in the endoplasmic reticulum (ER) and then transported to the cell membrane through a vesicular trafficking system. It undergoes various protein-protein interactions and interactions with chaperones to ensure its proper folding and transport to the target location.
Yes, AQP1 can be phosphorylated by different protein kinases, including protein kinase A (PKA) and protein kinase C (PKC). Phosphorylation of AQP1 can modulate its activity, cellular localization, and interaction with other proteins.
Customer Reviews (4)
Write a reviewthe manufacturer's technical expertise can be advantageous to researchers.
They can offer guidance on experimental design, protocol optimization, and troubleshooting, helping researchers overcome any challenges encountered during their trials.
This technical support is invaluable, especially for researchers who may be new to working with AQP1 protein or if they encounter specific difficulties while conducting their experiments.
This quality control is essential for obtaining reliable and reproducible data, as any variability in protein quality can introduce confounding factors into experiments.
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