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Brand: ProteoGenix

Recombinant Human P2RX6 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
33.02 kDa

$392.00

100ug + 392 loyalty points
Lys61–Gly333
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Recombinant Human P2RX6 Protein, N-His

Recombinant Human P2RX6 Protein, N-His

Product name Recombinant Human P2RX6 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 33.02 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Lys61-Gly333
Aliases /Synonyms Purinergic receptor, P2XM, Purinergic receptor P2X-like 1, P2RXL1, P2X purinoceptor 6, P2X6, ATP receptor, P2RX6
Reference ARO-P11592
Note For research use only.
Molecular Constructor
Lys61–Gly333

Introduction

Recombinant Human P2RX6 Protein is a type of protein that is produced through genetic engineering techniques. It is a member of the P2X purinergic receptor family, which are ion channels that are activated by extracellular ATP. P2RX6 is expressed in various tissues, including the brain, heart, and immune cells, and has been found to play a role in various physiological and pathological processes.

Structure of Recombinant Human P2RX6 Protein

Recombinant Human P2RX6 Protein is a transmembrane protein with a molecular weight of approximately 50 kDa. It is composed of 489 amino acids and has a predicted N-terminal signal peptide, two transmembrane domains, and a large extracellular loop. The extracellular loop contains the ATP-binding site, which is critical for the activation of the receptor.

Activity of Recombinant Human P2RX6 Protein

Recombinant Human P2RX6 Protein functions as an ion channel, allowing the passage of ions such as calcium and sodium across the cell membrane. This activity is regulated by the binding of ATP to the extracellular loop of the receptor. Upon ATP binding, the receptor undergoes a conformational change, leading to the opening of the ion channel and the influx of ions into the cell. This influx of ions can trigger various downstream signaling pathways, influencing cellular processes such as neurotransmission, immune response, and cell proliferation.

Application of Recombinant Human P2RX6 Protein

Recombinant Human P2RX6 Protein has been used in various research studies to investigate its role in different physiological and pathological processes. One such application is in the field of neuroscience, where P2RX6 has been found to play a role in pain perception and neuronal signaling. Studies have shown that P2RX6 is highly expressed in sensory neurons and is involved in the transmission of pain signals. Therefore, it has been suggested as a potential target for the development of novel analgesics.

In addition, P2RX6 has also been implicated in immune response and inflammation. It is expressed in various immune cells, and its activation has been linked to the release of pro-inflammatory cytokines. This suggests that P2RX6 may be involved in the pathogenesis of inflammatory diseases, making it a potential target for therapeutic intervention.

Furthermore, P2RX6 has also been studied in the context of cardiovascular diseases. It has been found to be expressed in cardiac cells and has been shown to regulate cardiac contractility. Dysfunction of P2RX6 has been associated with various cardiac disorders, including heart failure and arrhythmias. Therefore, targeting P2RX6 may have therapeutic potential in the treatment of these conditions.

Conclusion

In summary, Recombinant Human P2RX6 Protein is a transmembrane protein that functions as an ion channel and is activated by extracellular ATP. It is involved in various physiological and pathological processes, including pain perception, immune response, and cardiovascular function. Its potential as a therapeutic target in various diseases makes it a promising area of research. Further studies on the structure and activity of P2RX6 may provide valuable insights into its role in different processes and aid in the development of novel treatments.

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