UBL4B inhibitors are chemical agents that target and impede the activity of the ubiquitin-like protein 4B (UBL4B), a member of the ubiquitin-like protein family. The inhibition process typically involves the molecular interaction between the inhibitor and specific sites on the UBL4B protein, which disrupts its natural function. This interaction can be competitive, non-competitive, or uncompetitive, depending on whether the inhibitor directly competes with the natural substrate or ligand of UBL4B, binds to a separate site to induce a conformational change, or interacts only when the protein is in a complex with its substrate, respectively. The design of UBL4B inhibitors is a sophisticated task that requires a comprehensive understanding of the protein's structure, the nature of its interaction with other cellular components, and the signaling pathways it is involved in. Advanced techniques such as molecular docking, virtual screening, and structure-activity relationship (SAR) studies are commonly employed to guide the chemical synthesis of these inhibitors, ensuring specificity and a high affinity for the UBL4B protein.
Within the realm of UBL4B inhibitors, structural diversity is vast, encompassing small organic molecules, peptides, and potentially larger biomolecule-based inhibitors. The molecular architecture of these inhibitors is critical, as it determines both the potency and selectivity of the inhibitor for the UBL4B protein. Researchers meticulously analyze the three-dimensional structure of UBL4B, taking into account factors such as the arrangement of amino acids in the active or binding sites, the protein's dynamic conformational states, and the potential for allosteric regulation. The interaction between UBL4B and its inhibitors is not merely a lock-and-key mechanism but often involves induced fit or conformational adaptations that allow for high-fidelity binding. The physicochemical properties of UBL4B inhibitors, such as solubility, stability, and the ability to traverse cellular membranes, are also pivotal considerations in their design.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $38.00 $58.00 $102.00 $202.00 | 8 | |
Geldanamycin binds to heat shock protein 90 (Hsp90) and inhibits its chaperone activity. Hsp90 is crucial for the stability and function of many client proteins, and by inhibiting Hsp90, UBL4B stability can be diminished. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
Withaferin A is a steroidal lactone that disrupts the cytoskeletal organization and induces the degradation of vimentin. Disruption of the cytoskeleton impairs cellular trafficking, potentially diminishing UBL4B function. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $56.00 $260.00 $980.00 | 163 | |
MG-132 is a proteasome inhibitor that prevents the degradation of ubiquitinated proteins, leading to cellular stress and potential downregulation of UBL4B due to the perturbation in proteostasis. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
Bortezomib is another proteasome inhibitor with a mechanism similar to MG-132. By preventing the proteasomal breakdown of proteins, it may indirectly decrease UBL4B activity through proteostatic stress. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $40.00 $82.00 $256.00 | 127 | |
Cycloheximide inhibits protein biosynthesis by interfering with the translocation step in protein synthesis, leading to reduced levels of newly synthesized proteins including UBL4B. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation. As glycosylation can affect protein folding and stability, this may indirectly affect UBL4B stability if it or its interacting proteins are glycosylated. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $62.00 $155.00 $320.00 | 233 | |
Rapamycin inhibits the mammalian target of rapamycin (mTOR) pathway, which is involved in protein synthesis and autophagy. This inhibition could lead to diminished synthesis and altered degradation of UBL4B. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine inhibits autophagy by preventing the acidification of lysosomes. This could result in altered protein degradation pathways, affecting the turnover and function of UBL4B. | ||||||
Puromycin dihydrochloride | 58-58-2 | sc-108071 sc-108071B sc-108071C sc-108071A | 25 mg 250 mg 1 g 50 mg | $40.00 $210.00 $816.00 $65.00 | 394 | |
Puromycin causes premature chain termination during protein synthesis, resulting in the production of truncated proteins. This action could lead to reduced levels of functional UBL4B. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $94.00 $349.00 | 114 | |
Thapsigargin is a sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) pump inhibitor, leading to disruption of calcium homeostasis. Disrupted calcium signaling may indirectly decrease UBL4B function. | ||||||