TIA1 Inhibitors
Chemical inhibitors of TIA1 can impact its function through various modes of action that target the protein synthesis machinery within cells. Anisomycin, for example, binds to the 60S ribosomal subunit, which is a critical component of the ribosome responsible for peptide bond formation during translation. By hindering peptidyl transferase activity, Anisomycin effectively blocks the translation process, leading to a reduction in the synthesis of proteins, including TIA1. Similarly, Cycloheximide exerts its effect by inhibiting the translocation step in protein synthesis on ribosomes. This step is pivotal for the continuation of protein elongation, and its inhibition by Cycloheximide leads to a decrease in the production of TIA1.
Emetine and Rocaglamide also disrupt protein synthesis but act at different stages. Emetine tightly binds to the 40S ribosomal subunit, interfering with the translocation of peptidyl-tRNA from the A to the P site, thereby impeding the translation process and reducing TIA1 synthesis. Rocaglamide, on the other hand, prevents the initiation stage of protein synthesis. It achieves this by binding to eIF4A, a critical factor for ribosome assembly on mRNA, thus indirectly reducing the synthesis of TIA1 by blocking the necessary components from coming together to begin translation. Silvestrol and Harringtonine target the initiation and elongation stages of protein synthesis, respectively. Silvestrol binds to eIF4A, much like Rocaglamide, disrupting the formation of the eIF4F complex, essential for the translation initiation process. Harringtonine binds to the A site of the 60S ribosomal subunit, preventing peptide bond formation, an early step in the elongation process, thereby resulting in decreased TIA1 synthesis. Homoharringtonine also targets the elongation process, albeit by preventing the incorporation of amino acids into the growing peptide chain. All these inhibitors ultimately lead to reduced TIA1 levels and function in the cell by diminishing or completely halting its synthesis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin inhibits protein synthesis by binding to the 60S ribosomal subunit, hindering peptidyl transferase activity. This leads to the inhibition of mRNA translation, which is essential for the synthesis of TIA1. As TIA1 is a RNA-binding protein, its function is hampered due to lack of synthesis, indirectly reducing the functional pool of TIA1 within the cell. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $41.00 $84.00 $275.00 | 127 | |
Cycloheximide acts by blocking the translocation step in protein synthesis on ribosomes, thereby inhibiting the synthesis of many proteins including TIA1. With the synthesis of TIA1 inhibited, the protein's cellular concentration and function are reduced. | ||||||
Emetine | 483-18-1 | sc-470668 sc-470668A sc-470668B sc-470668C | 1 mg 10 mg 50 mg 100 mg | $440.00 $900.00 $1400.00 $2502.00 | ||
Emetine, a protein synthesis inhibitor, can indirectly inhibit TIA1 by blocking its translation. Emetine tightly binds to the 40S ribosomal subunit, interfering with the translocation of peptidyl-tRNA from the A to the P site of the ribosome. This action prevents the production of new TIA1 protein, thus inhibiting its availability and function in the cell. | ||||||
Rocaglamide | 84573-16-0 | sc-203241 sc-203241A sc-203241B sc-203241C sc-203241D | 100 µg 1 mg 5 mg 10 mg 25 mg | $275.00 $474.00 $1639.00 $2497.00 $5344.00 | 4 | |
Rocaglamide inhibits protein translation initiation by binding to eIF4A and preventing its interaction with eIF4B and eIF4F, essential components for the ribosome assembly on mRNA. As TIA1 synthesis depends on efficient translation initiation, rocaglamide indirectly inhibits TIA1 by reducing its synthesis. | ||||||
Silvestrol | 697235-38-4 | sc-507504 | 1 mg | $920.00 | ||
Silvestrol is an inhibitor of translation initiation. It functions by binding to the DEAD-box helicase eIF4A, an essential factor in the ribosome recruitment process to mRNA. This binding impedes the assembly of the eIF4F complex, thereby diminishing the synthesis of proteins, including TIA1. Consequently, TIA1 function is indirectly inhibited due to its reduced synthesis. | ||||||
Harringtonin | 26833-85-2 | sc-204771 sc-204771A sc-204771B sc-204771C sc-204771D | 5 mg 10 mg 25 mg 50 mg 100 mg | $250.00 $367.00 $548.00 $730.00 $980.00 | 30 | |
Harringtonine inhibits protein synthesis by preventing the initial elongation step of translation. It does this by binding to the A site of the 60S ribosomal subunit, leading to the inhibition of peptide bond formation. This action results in a decrease in TIA1 synthesis, thereby indirectly inhibiting the protein’s function due to a lack of new protein production. | ||||||
Homoharringtonine | 26833-87-4 | sc-202652 sc-202652A sc-202652B | 1 mg 5 mg 10 mg | $52.00 $125.00 $182.00 | 11 | |
Homoharringtonine inhibits protein synthesis by binding to ribosomes and preventing the incorporation of amino acids into elongating peptide chains. This inhibition reduces the synthesis of proteins including TIA1, leading to its functional inhibition due to decreased cellular levels. | ||||||
Puromycin | 53-79-2 | sc-205821 sc-205821A | 10 mg 25 mg | $166.00 $322.00 | 436 | |
Puromycin causes premature chain termination during protein synthesis by acting as an analog of aminoacyl-tRNA, resulting in the release of incomplete polypeptide chains. This effect reduces the synthesis of all proteins, including TIA1, thereby indirectly inhibiting its function by preventing the production of functional TIA1 protein. | ||||||
α-Sarcin | 86243-64-3 | sc-204427 | 1 mg | $462.00 | 6 | |
Alpha-Sarcin is a ribosome-inactivating protein that cleaves a specific phosphodiester bond within the 28S rRNA of the ribosome, leading to the inhibition of the elongation factor-dependent translocation of peptidyl-tRNA during protein synthesis. This action results in decreased synthesis of proteins including TIA1, thereby inhibiting its function indirectly. | ||||||