FKBP14 Activators
FKBP14 Activators belong to a class of chemical compounds that interact with and modulate the activity of the protein known as FKBP14, which is a member of the immunophilin protein family. The FKBP14 protein, short for FK506 Binding Protein 14, is a small member of this family and, like others, is named after its ability to bind to the immunosuppressive drug FK506, although its natural functions extend beyond this interaction. These proteins typically possess peptidyl-prolyl isomerase activity, which means they can catalyze the cis-trans isomerization of proline imidic peptide bonds in polypeptides, influencing protein folding and function. FKBP14, in particular, is expressed in various tissues and is involved in processes that are critical to cellular function. The activators of FKBP14, therefore, are chemicals that can enhance the protein's natural activity, potentially influencing the various biological processes in which FKBP14 is involved.
These activators can be small organic molecules or other types of compounds that have been identified or designed to specifically interact with FKBP14. The precise mechanism by which they activate FKBP14 is typically determined by their structure and the nature of their interaction with the protein. This interaction may induce a conformational change in FKBP14, increasing its enzymatic activity, or it may stabilize the protein, prolonging its active state. The molecular design of FKBP14 activators requires a deep understanding of the protein's structure and the dynamics of its active site. This knowledge allows for the optimization of activator binding, either enhancing the protein's interaction with its natural substrates or modulating its activity in a more general sense. The specificity of these activators is crucial, as off-target effects can influence other members of the immunophilin family, leading to unintended consequences. As such, the development of FKBP14 activators is a fine-tuned process that seeks to precisely modulate the function of this particular protein without disturbing the delicate balance of the cellular environment.
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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 | $63.00 $92.00 $250.00 $485.00 $1035.00 $2141.00 | 69 | |
Cyclosporin A binds to the cyclophilin family of proteins, such as FKBP14, and can inhibit calcineurin, thereby leading to increased cellular stress responses which FKBP14 is known to modulate. This binding enhances FKBP14's peptidyl-prolyl isomerase activity, thus increasing its functional activity. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $63.00 $158.00 $326.00 | 233 | |
Rapamycin specifically binds to FKBP family proteins including FKBP14, inhibiting mTOR pathway. This results in a biological response to counter cellular stress, a reaction where FKBP14 is implicated. The interaction with rapamycin can enhance the chaperone activity of FKBP14. | ||||||
Collagen IV | sc-29010 | 1 mg | $224.00 | 11 | ||
Collagen interaction with FKBP14 is crucial in the context of extracellular matrix deposition. FKBP14, being associated with collagen processing, is activated in terms of its enzymatic action on collagen, enhancing its role in proper folding and assembly of collagen triple helices. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
As a cofactor, zinc can enhance the enzymatic activity of many proteins. In the context of FKBP14, zinc may enhance its catalytic efficiency regarding the isomerization of peptide bonds, a function central to FKBP14's role in extracellular matrix organization. | ||||||
Copper | 7440-50-8 | sc-211129 | 100 g | $51.00 | ||
Copper, like zinc, may serve as a cofactor and enhance the isomerase activity of FKBP14. The presence of copper can increase the functional activity of FKBP14, particularly in its interaction with collagen and elastin, both key components of the extracellular matrix. | ||||||
Dimethyl Sulfoxide (DMSO) | 67-68-5 | sc-202581 sc-202581A sc-202581B | 100 ml 500 ml 4 L | $31.00 $117.00 $918.00 | 136 | |
DMSO may affect protein folding and stability. It can, therefore, be used to enhance the chaperone-like activity of FKBP14, which is involved in protein folding in the endoplasmic reticulum, ensuring proper protein conformation and function. | ||||||
Hydrogen Peroxide | 7722-84-1 | sc-203336 sc-203336A sc-203336B | 100 ml 500 ml 3.8 L | $31.00 $61.00 $95.00 | 28 | |
As an inducer of oxidative stress, hydrogen peroxide can upregulate the activity of proteins involved in counteracting this stress, including FKBP14. FKBP14 can be indirectly activated in response to oxidative conditions to enhance its chaperone activity to maintain cellular homeostasis. | ||||||
Retinoic Acid, all trans | 302-79-4 | sc-200898 sc-200898A sc-200898B sc-200898C | 500 mg 5 g 10 g 100 g | $66.00 $325.00 $587.00 $1018.00 | 28 | |
Retinoic acid influences gene expression and can lead to the upregulation of stress response proteins. FKBP14, being part of the cellular stress response machinery, may have its functional activity indirectly enhanced through retinoic acid-induced signaling pathways. | ||||||
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin binds to Hsp90, influencing protein folding pathways. As FKBP14 is involved in similar pathways, geldanamycin may indirectly enhance FKBP14's activity by modulating the protein folding environment in which FKBP14 operates, thereby increasing its functional activity in chaperoning. | ||||||
Cholecalciferol | 67-97-0 | sc-205630 sc-205630A sc-205630B | 1 g 5 g 10 g | $71.00 $163.00 $296.00 | 2 | |
Vitamin D3 is involved in the regulation of a wide array of genes, including those related to stress response and protein folding. FKBP14, being a part of these processes, may have its activity indirectly enhanced by the holistic effects of vitamin D3 on cellular homeostasis and stress responses. | ||||||