Ion channels are pore-forming proteins that allow the flow of ions across membranes, either plasma membranes or the membranes of intracellular organelles. Many ion channels (such as most Na, K Ca and some Cl channels) are gated by voltage but others (such as certain K and Cl channels, TRP channels, ryanodine receptors and IP3 receptors) are relatively voltage-insensitive and are gated by second messengers and other intracellular and/or extracellular mediators.
Most ion channels are highly selective for the class of ions crossing the channel. They can therefore be easily classified into sodium channels, calcium channels, potassium channels, proton channels or non-selective cation channels. Research on ion channels requires a large number of methods and materials. We offer monoclonal and polyclonal antibodies, ELISA kits and high-quality made-to-order proteins for this complex topic.
Aquaporins (often called aquaporin water channels) are a family of small, integral membrane proteins that are expressed broadly throughout the animal and plant kingdoms. They have a similar basic structure, with aquaporin monomers consisting of six transmembrane helical segments and two short helical segments that surround cytoplasmic and extracellular vestibules connected by a narrow aqueous pore.
To search our Aquaporin antibodies, kits, proteins click on the links below.
A calcium channel is a transmembrane ion channel that is permeable to calcium ions. The permeability is controlled either by voltage-gated calcium channels or ligand-gated calcium channels. We offer some hand-picked monoclonal and polyclonal antibodies for research on calcium channels.
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Potassium channels ubiquitously exist in nearly all kingdoms of life and perform diverse but important functions. Since the first atomic structure of a prokaryotic potassium channel (KcsA, a channel from Streptomyces lividans) was determined, tremendous progress has been made in understanding the mechanism of potassium channels and channels conducting other ions.
There are two major classes of sodium channels in mammals: The voltage-gated sodium channel (VGSC) family and the epithelial sodium channel (ESC). Voltage-gated sodium channels exist throughout the body in various cell types, while epithelial sodium channels are located primarily in the skin and kidney.
Transient receptor potential (TRP) channels are nonselective cationic channels, conserved among flies to humans. Most TRP channels have well known functions in chemosensation, thermosensation, and mechanosensation. In addition to being sensing environmental changes, many TRP channels are also internal sensors that help maintain homeostasis.
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Cyclic Nucleotide-gated Ion Channels
Cyclic nucleotide-gated (CNG) channels are nonselective cation channels first identified in retinal photoreceptors and olfactory sensory neurons (OSNs). They are opened by the direct binding of cyclic nucleotides, cAMP and cGMP. Although their activity shows very little voltage dependence, CNG channels belong to the superfamily of voltage-gated ion channels. Below you will find a selection of polyclonal antibodies against CNG ion channels.
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Hyperpolarization-activated Cyclic Nucleotide-gated Channels (HCN)
A hyperpolarization-activated cyclic nucleotide-gated channel (HCN) is a subtype of CNG channel that is gated by hyperpolarization of the cell membrane. There are four HCN channels HCN1, HCN2, HCN3, and HCN4.
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We offer you Made-to-order Channel Proteins
We offer high-purity made-to-order ion channel proteins with native state folding guarantee. Below you will find a selection of potassium channel proteins. Please contact us via email, chat, or phone for more information about our made-to-order proteins.
References:: "Aquaporins." in: Current biology : CB, Vol. 23, Issue 2, pp. R52-5, (2013) (PubMed).
: "Structure of potassium channels." in: Cellular and molecular life sciences : CMLS, Vol. 72, Issue 19, pp. 3677-93, (2015) (PubMed).
: "Transient Receptor Potential Channels and Metabolism." in: Molecules and cells, Vol. 42, Issue 8, pp. 569-578, (2020) (PubMed).
: "Cyclic nucleotide-gated ion channels." in: Physiological reviews, Vol. 82, Issue 3, pp. 769-824, (2002) (PubMed).