Pin1l Activators
PIN1P1, or peptidylprolyl cis/trans isomerase, NIMA-interacting 1 pseudogene 1, is a unique entity in the realm of protein biochemistry and cell signaling. As a pseudogene-derived protein, PIN1P1 potentially shares functional similarities with its ancestral gene, PIN1, which is known for its critical role in mediating the cis-trans isomerization of prolyl bonds in phosphorylated Ser/Thr-Pro motifs. This isomerization is essential for the regulation of various cellular processes, including cell cycle progression, signal transduction, and protein folding. The exact biochemical functions and pathways involving PIN1P1, however, are not as well characterized as those of PIN1, leaving room for exploration and discovery. The functional activation of PIN1P1, as hypothesized, would likely involve the modulation of protein-protein interactions and the regulation of substrate proteins through isomerization, akin to PIN1. Activation of PIN1P1 would therefore be intricately linked to the phosphorylation state of its substrates. Chemicals that indirectly increase the phosphorylation levels of these substrates can, therefore, be considered potential activators of PIN1P1. These activators operate predominantly by inhibiting phosphatases or modulating kinase activity, leading to an increased pool of phosphorylated proteins. This increase in phosphorylation can enhance the interaction between PIN1P1 and its substrates, thereby potentially augmenting its isomerase activity.
In the cellular context, the activation of PIN1P1 through such indirect mechanisms suggests its involvement in complex signaling cascades where phosphorylation and dephosphorylation events are key. The chemicals listed, while not directly interacting with PIN1P1, create a cellular environment conducive to its activation by manipulating the phosphorylation landscape. This manipulation affects various signaling pathways, potentially including those directly involving PIN1P1, thus indirectly facilitating its functional role. Understanding the nuances of PIN1P1 activation, particularly in the context of its pseudogene origin, opens new avenues for exploring its biological significance and potential implications in cellular processes.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cyclosporin A | 59865-13-3 | sc-3503 sc-3503-CW sc-3503A sc-3503B sc-3503C sc-3503D | 100 mg 100 mg 500 mg 10 g 25 g 100 g | $62.00 $90.00 $299.00 $475.00 $1015.00 $2099.00 | 69 | |
Cyclosporin A, an immunosuppressant, inhibits the phosphatase activity of calcineurin. This inhibition indirectly activates PIN1P1 by reducing the dephosphorylation of PIN1P1 substrates, thus maintaining their proline-directed phosphorylation state, which is a prerequisite for PIN1P1 activity. | ||||||
FK-506 | 104987-11-3 | sc-24649 sc-24649A | 5 mg 10 mg | $76.00 $148.00 | 9 | |
FK506, another immunosuppressant, binds to FKBP12, forming a complex that inhibits calcineurin. This inhibition leads to an indirect activation of PIN1P1, as it preserves the phosphorylation of proline-directed motifs in PIN1P1 substrates, essential for PIN1P1's isomerase activity. | ||||||
Juglone | 481-39-0 | sc-202675 sc-202675A | 1 g 5 g | $66.00 $222.00 | 6 | |
Juglone, a natural naphthoquinone, is known to inhibit PTPs (Protein Tyrosine Phosphatases). This inhibition leads to an increase in tyrosine phosphorylation, a post-translational modification that can indirectly activate PIN1P1 by increasing the interaction and isomerization of its substrates. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic Acid, a potent inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A), leads to hyperphosphorylation of proteins. This hyperphosphorylation indirectly activates PIN1P1 by increasing the availability of phosphorylated substrates, which are necessary for PIN1P1's catalytic activity. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $45.00 $56.00 $183.00 | 142 | |
Sodium Orthovanadate is a general inhibitor of protein tyrosine phosphatases. It causes an increase in tyrosine-phosphorylated proteins, indirectly promoting PIN1P1 activation by enhancing the phosphorylation status of PIN1P1's substrates, thereby facilitating their isomerization. | ||||||
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
Staurosporine, a kinase inhibitor, paradoxically can induce hyperphosphorylation under certain conditions. This hyperphosphorylation indirectly activates PIN1P1 by increasing the phosphorylation of its substrates, which is crucial for PIN1P1's peptidyl-prolyl isomerase 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, an inhibitor of protein phosphatases PP1 and PP2A, induces protein hyperphosphorylation. This hyperphosphorylation indirectly activates PIN1P1 by augmenting the pool of phosphorylated substrates necessary for PIN1P1 to exert its isomerase activity. | ||||||
Phenylarsine oxide | 637-03-6 | sc-3521 | 250 mg | $40.00 | 4 | |
Phenylarsine Oxide, an inhibitor of protein tyrosine phosphatases, indirectly activates PIN1P1. By inhibiting the dephosphorylation of tyrosine residues, it increases phosphorylated substrate availability for PIN1P1, facilitating its isomerase function. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
Epigallocatechin Gallate, a polyphenol in green tea, has been shown to inhibit multiple protein phosphatases. This inhibition leads to an increase in phosphorylated proteins, indirectly activating PIN1P1 by enhancing the phosphorylation status of its substrates. | ||||||
Cantharidin | 56-25-7 | sc-201321 sc-201321A | 25 mg 100 mg | $81.00 $260.00 | 6 | |
Cantharidin, a natural toxin, inhibits protein phosphatases PP1 and PP2A. This inhibition results in increased phosphorylation of proteins, indirectly activating PIN1P1 by elevating the phosphorylation level of its substrates, crucial for PIN1P1's activity. | ||||||