SKCa Related Drug Discovery Products

Low intracellular Ca²⁺ concentrations can activate SKCa channels, which are small conductance calcium-activated K⁺ channels that are not voltage-dependent. A Ca²⁺ calmodulin binding site in the intracytoplasmic C-terminal region mediates their high sensitivity to Ca²⁺. SKCa, which has a high Ca²⁺ sensitivity, regulates Ca-dependent signaling pathways in both excitable and non-excitable cells. The amount of Ca²⁺ inside cells can change depending on how the resting membrane potential is regulated. In excitable cells, like neurons, the activation of these channels typically results in repolarization or hyperpolarization, which shuts down voltage-gated Ca²⁺ channels or reduces the likelihood that they will open, lowering intracellular Ca²⁺ concentration.

Creative Biolabs is proud to offer our clients a series of SKCa drug discovery tools with the best quality and most competitive price:

• SKCa Assays
• Ion Channel Cell Lines
• Ion Channel Membranes
• Membrane Protein Tools

Overview of SKCa

SKCa is encoded by three full sequences: SK1, SK2, and SK3. The three components' sequences are 70 to 80 percent identical. They are, however, only 15% identical to the sequences of the BKCa channel subunits and 40% to 50% identical to those of the IKCa channel α-subunit.

• SK1

The SK1 generates at least four splice variants in people and 16 in rodents, which result in the synthesis of many protein isoforms, including the functional version. In reticulocytes, leukemia cells, and the hippocampus of humans, three shortened splicing variants of the C-terminus with the calmodulin binding site have been discovered. This hippocampus variant, which has 18 more amino acids, has been seen in the brains of human embryos.

• SK2

There have been three different types of SK2 identified: SK2-S, SK2-L, and SK2-sh. The only difference between the SK2-L and SK2-S is the extra 207 amino acids that the SK2-L has at its N terminus. Separately expressed SK2-S and SK2-L in COS cells result in functional channels with comparable Ca²⁺ sensitivity. Potential regulatory regions that could alter the channel's activity and location at the plasma membrane can be found in the extended N-terminus of SK2-L. The third form, SK2-sh, is an SK2-S splice variant with 140 amino acids missing, which correspond to the S3, S4, and S5 segments. SK2-sh levels are higher in Alzheimer's disease patients' brains than in controls' brains, but its exact function is unclear.

• SK3

A polymorphic CAG repeat in the N-terminal coding region of the SK3 gene serves as its defining feature. Longer polyglutamine lengths have recently been found to influence channel conductance but not the location of the SK3 channel in the cell membrane. Lower current amplitudes at depolarized potentials are correlated with longer CAG repetitions. The acute neurotoxicity of oxaliplatin has been linked to the SK3 gene's polymorphism CAG motif.