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Agrisera
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Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
For reconstitution add 100 µL of sterile water.
Specific Species Reactivity: Natronomonas pharaonis
NpHR encodes a microbial rhodopsin from the haloarchaeon Natronomonas pharaonis that is embedded in the cell membrane as a retinylidene protein with seven transmembrane helices (A-G) and an N-terminal amphipathic helix (A') that, together with an extended extracellular loop between helices B and C, forms a cap over the extracellular face of the protein. The chromophore retinal is covalently linked to a conserved lysine in helix G via a protonated Schiff base positioned near a primary chloride-binding site, where the anion is stabilized by polar residues (including Thr126 and Ser130) adjacent to the Schiff base. Structurally, NpHR assembles as a trimer, and light absorption drives retinal isomerization and a photocycle that results in active transport of a halide ion (preferentially chloride) from the extracellular side to the cytoplasmic side. Functionally, this inward light-driven chloride pumping alters the transmembrane electrochemical gradient (hyperpolarizing when expressed in heterologous membranes), and targeted mutagenesis and electrophysiology support a key role for residues near the Schiff base region (e.g., Ser81 influencing Thr126-mediated anion coordination) in enabling efficient chloride migration through the protein.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: eNpHR; eNpHR3.0; halorhodopsin; HR; Natronomonas pharaonis halorhodopsin; pharaonis halorhodopsin; phR