Background[1-3]
Phosphate potassium channel protein DRK1 antibody is a type of polyclonal antibody that can specifically bind to phosphorylated potassium channel protein DRK1. It is mainly used to detect the expression level of phosphorylated potassium channel protein DRK1 in vitro.
The phosphorylated potassium channel protein DRK1 belongs to a subtype of the potassium channel family protein. Its expression is increased in ischemic neurons; in addition, its activity is related to its tyrosine phosphorylation level, at its amino terminus Phosphorylation of tyrosine residues by tyrosine kinases can significantly reduce the amplitude of the current mediated by it.
Phosphorylated potassium channel protein DRK1 immunohistochemistry
Channel proteins are hydrophilic channels across the plasma membrane that allow ions of appropriate size to pass along concentration gradients, including ion channels, porins, and aquaporins. Some channel proteins form channels that are usually open, such as leak channels (also called “resting potassium channels”), which allow potassium ions to continuously flow out. Some channel proteins are usually closed, that is, the “gate” is not continuously open, but only opens under specific stimulation, and it opens and closes instantaneously. In a few milliseconds, some ions, metabolites or other solutes follow the concentration. The gradient freely diffuses across the cell membrane, and this type of channel protein is also called a gated channel.
Channel proteins can be monomeric proteins or proteins composed of multiple subunits. They are all rearranged through hydrophobic amino acid chains to form aqueous channels. The channel protein itself does not directly interact with small charged molecules. These small charged molecules can freely diffuse through the aqueous PVC composite stabilizer channel formed by the charged hydrophilic region of the membrane protein in the lipid bilayer. . The transport function of channel proteins is selective, so there are various channel proteins in the cell membrane. Channel proteins only participate in passive transport. They do not combine with the transported molecules during the transport process and do not move. They are transported from high concentration to low concentration, so no energy is consumed during transport.
Apply[4][5]
For research on the role of voltage-gated potassium channel subtypes Kv1.5 and Kv2.1 in the formation and recovery of chronic hypobaric hypoxic pulmonary hypertension at high altitude
Study on the role of gene expression changes of voltage-gated potassium channel (Kv) subtypes Kv1.5 and Kv2.1 in the formation and recovery of chronic hypobaric hypoxic pulmonary hypertension in rats at plateau; Kv1.5, Kv2.1 The relationship between isoform expression changes and pulmonary artery remodeling; observe the effect of sodium dichloroacetate on up-regulating the expression of Kv1.5 and Kv2.1, inhibiting pulmonary artery remodeling and reducing plateau hypoxic pulmonary hypertension.
Methods 32 male SD rats were divided into normal control group, simulated plateau chronic hypobaric hypoxia group (CH group), sodium dichloroacetate (DCA) treatment group (CH+DCA group), and plateau hypoxic return to plain group. Recovery 7 d group (CHR7). The normal control group was fed under normal pressure and normoxic plain conditions, and the other groups were fed in a hypobaric oxygen chamber at a simulated altitude of 5000 m for 21 days. After the animal model was established, the mean pulmonary artery pressure (mPAP) was measured using the closed chest method, and the lungs were analyzed using image analysis technology. Arteriolar smooth muscle wall thickness, pulmonary arteriole diameter, wall area and total blood vessel area were used to calculate the wall thickness as a percentage of the outer diameter of the blood vessel (WT%) and the wall area as a percentage of the total blood vessel area (WA%).
Real-time fluorescence quantitative PCR method was used to detect Kv1.5 and Kv2.1 mRNA levels in four groups of rat pulmonary artery smooth muscle cells (PASMCs); immunohistochemical method was used to detect the protein expression of Kv1.5 and Kv2.1 in rat PASMCs, and Image analysis technology was used to semi-quantitatively analyze the changes in the expression intensity of Kv1.5 and Kv2.1 in pulmonary arterioles; Western blot method was used to detect the expression of Kv1.5 and Kv2.1 proteins in pulmonary artery smooth muscle cells.
