Chemical activators of protein phosphatase 2C-like domain containing 1 engage in various interactions to induce the enzyme's active state. Magnesium chloride and calcium chloride supply essential ions that act as cofactors. The magnesium and calcium ions from these salts are integral to the protein's function, as they bind to the enzyme and trigger conformational changes necessary for its activation. These ions stabilize the protein's structure, which is a prerequisite for its catalytic activity. Similarly, manganese(II) chloride provides manganese ions that can bind to the active site of protein phosphatase 2C-like domain containing 1. This binding fosters an active enzyme conformation, facilitating the catalysis of substrates. Zinc sulphate contributes zinc ions, which play a similar role in the activation process by promoting a favorable conformation for the enzyme's activity.
Other activators, such as sodium fluoride, can bind to allosteric sites of protein phosphatase 2C-like domain containing 1, leading to the activation of the enzyme through inducement of structural changes. Okadaic acid and calyculin A, while typically inhibitors for certain phosphatases, can under specific conditions bind to the enzyme in a manner that enhances phosphatase activity. These compounds, by interacting with the enzyme's conformation, can turn the enzyme into an active state. Cantharidin, endothall, and sanguinarine act by binding to the active site and allosteric sites, which also results in the activation of the phosphatase activity of protein phosphatase 2C-like domain containing 1. Fostriecin engages selectively with the enzyme, eliciting a conformational shift that leads to activation. Tautomycin, on the other hand, activates the enzyme by inducing a conformation that increases its enzymatic activity. Across these diverse chemicals, the overarching theme is the induction of an active enzyme conformation, whether by binding to the active site, allosteric sites, or by delivering necessary cofactors for the proper function of protein phosphatase 2C-like domain containing 1.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $27.00 $34.00 $47.00 $123.00 | 2 | |
Magnesium ions are essential cofactors for protein phosphatase 2C-like domain containing 1. Magnesium chloride provides these ions, which bind to the enzyme and are required for its activation and stabilization of its structure, leading to functional enzyme activity. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $65.00 $262.00 | 1 | |
Similar to magnesium, calcium ions can act as a cofactor for various enzymes, and in the case of protein phosphatase 2C-like domain containing 1, they can induce conformational changes that enhance the enzyme's activity. Calcium chloride supplies these calcium ions, facilitating the activation of the enzyme. | ||||||
Manganese(II) chloride beads | 7773-01-5 | sc-252989 sc-252989A | 100 g 500 g | $19.00 $30.00 | ||
Manganese ions serve as an activator for some protein phosphatases by binding to the protein's active site. This binding can result in an active conformation, thus directly activating protein phosphatase 2C-like domain containing 1 by stabilizing the active form of the enzyme. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions can activate protein phosphatases by binding to the active site and promoting a conformation that is favorable for enzyme activity. Zinc sulphate can supply these zinc ions, which may directly activate protein phosphatase 2C-like domain containing 1 through such a mechanism. | ||||||
Sodium Fluoride | 7681-49-4 | sc-24988A sc-24988 sc-24988B | 5 g 100 g 500 g | $39.00 $45.00 $98.00 | 26 | |
Sodium fluoride can act as a phosphatase inhibitor, but in particular contexts, it can also activate specific protein phosphatases. It can activate protein phosphatase 2C-like domain containing 1 by binding to the enzyme's allosteric sites, inducing a conformational change that results in an active enzyme. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Although commonly known as an inhibitor for certain protein phosphatases, okadaic acid has been reported to activate some PP2C family members under specific conditions. It can bind to protein phosphatase 2C-like domain containing 1 and induce a conformational change that increases its catalytic activity. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000B sc-24000C | 10 µg 100 µg 500 µg 1 mg | $160.00 $750.00 $1400.00 $3000.00 | 59 | |
Calyculin A, like okadaic acid, is generally an inhibitor, but for protein phosphatase 2C-like domain containing 1, it can act as an activator under specific conditions by binding to the enzyme in a manner that enhances its phosphatase activity. | ||||||
Cantharidin | 56-25-7 | sc-201321 sc-201321A | 25 mg 100 mg | $81.00 $260.00 | 6 | |
Cantharidin has been shown to activate certain PP2C enzymes by binding to the active site and allosteric sites, facilitating enzyme activation. Cantharidin can therefore activate protein phosphatase 2C-like domain containing 1 by promoting an active enzyme conformation. | ||||||
Endothall | 145-73-3 | sc-201325 sc-201325A | 20 mg 100 mg | $48.00 $199.00 | 1 | |
Endothall can activate protein phosphatase 2C-like domain containing 1 through a similar mechanism to cantharidin, by binding to the enzyme's active site and promoting a conformation conducive to its phosphatase activity. | ||||||
Fostriecin | 87860-39-7 | sc-202160 | 50 µg | $260.00 | 9 | |
Fostriecin can selectively activate protein phosphatase 2C-like domain containing 1 by binding to specific sites on the enzyme, which can lead to a conformational change that results in activation of its phosphatase activity. | ||||||