Recombinant Mouse Ano9, His-tagged
Cat.No. : | Ano9-3503M |
Product Overview : | Anoctamin-9 (Ano9) |
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Source : | E. Coli or Yeast |
Species : | Mouse |
Tag : | His |
Form : | This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications. |
Protein length : | 747 |
Purity : | >90% |
Notes : | Small volumes of Ano9 recombinant protein may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice. |
Storage : | Store at -20 degree C. For extended storage, store at -20 or -80 degree C. |
Storage Buffer : | PBS pH 7.4, 50% glycerol |
Warning : | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Gene Name : | Ano9 anoctamin 9 [ Mus musculus ] |
Official Symbol : | Ano9 |
Synonyms : | Tp53i5; Tmem16j; Trp53i5; 5430425C04Rik; anoctamin-9; Trp53 inducible protein 5; transmembrane protein 16J; tumor protein p53 inducible protein 5; transformation related protein 53 inducible protein 5 |
Gene ID : | 71345 |
mRNA Refseq : | NM_178381 |
Protein Refseq : | NP_848468 |
UniProt ID : | P86044 |
Chromosome Location : | 7 F5; 7 |
Pathway : | Ion channel transport, organism-specific biosystem; Stimuli-sensing channels, organism-specific biosystem |
Function : | NOT intracellular calcium activated chloride channel activity; phospholipid scramblase activity |
Products Types
◆ Recombinant Protein | ||
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ANO9-948HCL | Recombinant Human ANO9 Cell Lysate | +Inquiry |
ANO9-3502H | Recombinant Human ANO9, His-tagged | +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 (27)
Ask a questionAlthough the exact functions of Ano9 protein in the peripheral nervous system are not completely understood, studies have suggested its potential involvement in pain sensation and neurotransmitter release at peripheral nerve terminals. Further research is needed to fully elucidate its roles in the peripheral nervous system.
Ano9 protein acts as a chloride channel, allowing the passage of chloride ions across cell membranes. These ions play a crucial role in regulating cell volume by controlling osmotic pressure and water movement.
Ano9 protein is primarily localized in the plasma membrane, where it functions as a chloride channel. However, it may also be present in intracellular compartments, although the significance of this subcellular distribution is not fully understood.
Yes, Ano9 protein is conserved across vertebrate species, suggesting its importance in physiological processes.
Ano9 is involved in various physiological processes, such as chloride ion transport, cell swelling regulation, and potentially other functions that are still being investigated.
Mutations in the ANO9 gene have been implicated in certain human disorders, such as autosomal recessive spinocerebellar ataxia 10 (SCAR10) and gnathodiaphyseal dysplasia.
Yes, Ano9 protein is known to be a member of the Ca2+-activated chloride channel (CaCC) family. It has been shown to function as a CaCC itself, mediating the transport of chloride ions across cell membranes. Ano9 has been implicated in various physiological processes where chloride ion transport is necessary, including fluid secretion, neuronal signaling, and electrolyte balance.
The specific cellular signaling pathways or cascades involving Ano9 protein are not yet fully characterized. However, some studies have suggested that it may interact with or be regulated by various signaling molecules, including calcium-dependent kinases and phosphatases. Further research is necessary to define its precise signaling interactions and downstream effects.
Currently, there are no specific drugs or inhibitors that exclusively target Ano9 protein. However, compounds that modulate chloride channels, in general, may affect its activity.
Apart from spinocerebellar ataxia 10 (SCAR10), which is associated with ANO9 mutations, there are currently no other known genetic disorders specifically linked to ANO9 gene mutations. However, as research on ANO9 continues, it is possible that additional genetic disorders may be identified.
Yes, Ano9 has been reported to interact with several regulatory proteins and ion channels, although the full extent of its interacting partners is yet to be fully characterized.
While the modulation of Ano9 protein activity is not well understood, some studies have reported potential agonists or modulators. For example, calcium ions have been shown to activate Ano9 channel activity. Other factors, such as changes in pH or phosphorylation status, may also influence Ano9 activity. However, further research is needed to fully elucidate the physiological regulation of Ano9 protein.
There is limited evidence suggesting that alterations in Ano9 protein expression or activity may impact immune system function or immune responses. Some studies have indicated its involvement in immune cell activation, cytokine release, and immune response modulation. However, more studies are needed to fully understand the role of Ano9 in immune function.
Mutations in the ANO9 gene have been associated with autosomal recessive spinocerebellar ataxia 10 (SCAR10). This genetic disorder affects the coordination and balance of movement, leading to progressive ataxia.
There are limited studies investigating the specific protein-protein interactions or associations of Ano9. However, some studies have reported potential interactions with other chloride channels, calcium-binding proteins, and signaling molecules. Further research is needed to fully understand the protein interaction network of Ano9.
The development of specific small molecule inhibitors or drugs targeting Ano9 protein is still in the early stages. Although there have been some studies exploring potential inhibitors, no approved therapeutic interventions directly targeting Ano9 are currently available. Further research is needed to determine the feasibility of developing such treatments.
Dysregulation of Ano9 protein expression or activity has been implicated in various diseases and conditions, including neurodegenerative disorders, cardiovascular diseases, and certain types of cancer. However, the exact mechanisms and consequences of such dysregulation in these diseases are still being investigated.
Yes, some studies have suggested a potential role for Ano9 protein in cancer progression and metastasis. It has been shown to be overexpressed in certain types of cancer, including breast, lung, and prostate cancer. Ano9 expression has been associated with increased tumor cell migration, invasion, and metastasis. Further research is underway to determine the underlying mechanisms and potential therapeutic implications.
Ano9 protein consists of multiple transmembrane domains, as well as a calcium-binding EF-hand motif essential for its activation.
The downstream signaling pathways activated by Ano9 are not fully elucidated. However, studies have suggested its involvement in intracellular calcium signaling, which could potentially regulate a variety of cellular processes.
Ano9 has been reported to be expressed in cardiac tissues and may play a role in cardiac function and arrhythmias. However, its precise involvement in the cardiovascular system is still being actively researched.
While the primary function of Ano9 protein is ion transport, recent studies have suggested its involvement in other processes, such as cell proliferation, apoptosis, and possibly immune responses. However, further investigation is necessary to determine the extent of its involvement in these activities.
Yes, Ano9 is a calcium-activated chloride channel. An increase in intracellular calcium levels leads to the binding of calcium to the EF-hand motif in Ano9, resulting in its activation and increased chloride ion conductance.
Although mutations in the ANO9 gene have been linked to spinocerebellar ataxia 10, which is neurodegenerative in nature, there is currently limited evidence suggesting a direct association between ANO9 mutations and channelopathies or other ion channel-related disorders. Further studies are needed to investigate the potential impact of ANO9 mutations on ion channel function and related disorders.
There is limited evidence suggesting that alterations in Ano9 protein expression or activity may impact cell migration and invasion in certain contexts. Some studies have reported its involvement in cell adhesion and invasion processes in cancer cells. However, more research is needed to fully understand the significance of Ano9 in these cellular processes.
The expression and regulation of Ano9 protein can be influenced by various factors. Studies have shown that its expression can be regulated by transcription factors, intracellular signaling pathways, and certain microRNAs. Additionally, external factors such as hypoxia, oxidative stress, and inflammatory signals can also modulate Ano9 expression. The precise mechanisms involved in its regulation are still being investigated.
Currently, there are limited animal models available specifically targeting Ano9 protein. Most research on Ano9 has utilized cell culture or ex vivo studies. However, the generation of animal models, such as knockout mice, could provide valuable insights into the physiological roles and relevance of Ano9 in vivo.
Customer Reviews (4)
Write a reviewts reliability and high quality make it a valuable tool in various applications, ranging from enzymatic assays to studying protein-protein interactions.
Its versatility and reliability make it a great choice for researchers exploring protein dynamics, function, and interactions.
the Ano9 protein is highly regarded for its excellent performance in WB assays and its significant contribution to protein EM structure analysis.
Its use in EM studies allows researchers to gain insights into the structural details of proteins and their complexes at high resolution.
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