ZIP3 Inhibitors
Chemical inhibitors of the zinc transporter protein ZIP3 can interfere with its function through various mechanisms, primarily by targeting cysteine residues and zinc-binding sites that are essential for the protein's activity. MTSEA, for instance, selectively modifies accessible cysteine residues, which are crucial for the structural integrity of ZIP3. By alkylating these residues, MTSEA can inhibit ZIP3 by disrupting its structural integrity or interfering with its ion transport mechanism. Similarly, iodoacetamide and N-Ethylmaleimide also alkylate cysteine residues, potentially leading to the inhibition of ZIP3 activity through conformational disruption. Phenylarsine Oxide, by binding to vicinal dithiols within the protein structure, can inhibit the function of cysteine-rich proteins like ZIP3 if intact dithiol groups are necessary for its function.
Other inhibitors affect ZIP3 function by altering zinc availability or mimicking its binding. Cadmium Chloride, for example, can replace zinc ions in proteins, inhibiting zinc-requiring enzymes like ZIP3 through competitive inhibition. TPEN, a high-affinity zinc chelator, depletes the substrate necessary for ZIP3's activity, thus inhibiting its function. DTNB, by reacting with free thiol groups, can modify essential thiol groups and disrupt ZIP3 activity. Pyrithione Zinc disrupts zinc homeostasis, which can indirectly inhibit ZIP3's zinc transport activity. Ziram, a dithiocarbamate pesticide, chelates zinc ions, potentially reducing the availability of zinc for ZIP3 to transport. Dipicolinic Acid, by chelating zinc, deprives ZIP3 of its essential metal ion, leading to functional inhibition. Quercetin can inhibit metal ion transporters by binding to metal-binding sites, which suggests it could alter the critical metal-binding site of ZIP3. Lastly, Ebselen, with its thiol-modifier properties, can modify specific thiol groups essential for ZIP3's activity and inhibit its function.
Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
MTSEA Biotin | 162758-04-5 | sc-221960 | 10 mg | $209.00 | ||
MTSEA selectively modifies accessible cysteine residues, and ZIP3 is known to have critical cysteine residues within its structure that are important for function. Alkylation of these residues by MTSEA would inhibit ZIP3 by disrupting its structural integrity or interfering with its ion transport mechanism. | ||||||
α-Iodoacetamide | 144-48-9 | sc-203320 | 25 g | $250.00 | 1 | |
Iodoacetamide alkylates cysteine residues in proteins, and if ZIP3 contains cysteine residues critical to its active site or structural conformation, modification by iodoacetamide would result in the inhibition of ZIP3 activity due to conformational disruption. | ||||||
N-Ethylmaleimide | 128-53-0 | sc-202719A sc-202719 sc-202719B sc-202719C sc-202719D | 1 g 5 g 25 g 100 g 250 g | $22.00 $68.00 $210.00 $780.00 $1880.00 | 19 | |
N-Ethylmaleimide reacts with free sulfhydryl groups on cysteine residues. If ZIP3 relies on the reactivity of such residues for zinc transport, the covalent modification by N-Ethylmaleimide would inhibit the protein's function. | ||||||
Phenylarsine oxide | 637-03-6 | sc-3521 | 250 mg | $40.00 | 4 | |
Phenylarsine Oxide binds to vicinal dithiols within protein structure and is commonly used to inhibit the function of cysteine-rich proteins. If ZIP3 requires intact dithiol groups for function, binding by Phenylarsine Oxide would inhibit its activity. | ||||||
Cadmium chloride, anhydrous | 10108-64-2 | sc-252533 sc-252533A sc-252533B | 10 g 50 g 500 g | $55.00 $179.00 $345.00 | 1 | |
Cadmium ions can replace zinc ions in proteins and can serve as potent inhibitors of zinc-requiring enzymes. If ZIP3's function involves the binding or transport of zinc, cadmium ions could directly inhibit this process by competitive inhibition. | ||||||
TPEN | 16858-02-9 | sc-200131 | 100 mg | $127.00 | 10 | |
TPEN (N,N,N',N'-Tetrakis(2-pyridylmethyl)ethylenediamine) is a high-affinity zinc chelator. If ZIP3's activity involves zinc handling, chelation of zinc by TPEN would inhibit ZIP3's function by depleting its substrate. | ||||||
5,5′-Dithio-bis-(2-nitrobenzoic Acid) | 69-78-3 | sc-359842 | 5 g | $78.00 | 3 | |
DTNB (5,5'-Dithiobis(2-nitrobenzoic acid)) reacts with free thiol groups in proteins. If ZIP3 has essential thiol groups for activity, DTNB would inhibit ZIP3 by modifying these groups, disrupting function. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Pyrithione Zinc is known to disrupt zinc homeostasis and could inhibit ZIP3 by altering the zinc concentrations that are necessary for the protein's normal function, thus indirectly inhibiting its transport activity. | ||||||
2,6-Pyridinedicarboxylic acid | 499-83-2 | sc-238430 sc-238430A sc-238430B sc-238430C | 5 g 100 g 1 kg 10 kg | $33.00 $92.00 $714.00 $6457.00 | ||
Dipicolinic Acid is a terdentate ligand that can chelate metal ions like zinc. If ZIP3 activity is dependent on zinc, the chelation of zinc by Dipicolinic Acid would result in functional inhibition by depriving ZIP3 of its essential metal ion. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $108.00 $245.00 $918.00 $49.00 | 33 | |
Quercetin has been shown to inhibit metal ion transporters by binding to metal-binding sites. If ZIP3 activity involves a metal-binding site that is critical for its function, Quercetin could inhibit ZIP3 by occupying or altering this site. | ||||||