FKBPs (FK506-binding proteins) interact with immunosuppressants like FK506 and Rapamycin. They are a special class of immunophilins. During protein folding processes, FKBPs use their peptidyl-prolyl isomerase (PPIase) activity to catalyze the cis-trans conversion of prolyl bonds in proteins. The FKBPs serve as an exceptional group of chaperones. Protein folding, receptor signaling, protein trafficking, and transcription are just a few of the biochemical processes that FKBPs are involved in. When they are complexed with their ligands, proteins from the FKBP family have significant functional roles in the activation of T cells.
Through their interactions with kinases, steroid hormone receptors, and other cellular components, FKBPs contribute significantly to a number of physiological processes and, more intriguingly, to pathological processes in mammals. Four categories—cytoplasmic, TPR domain, endoplasmic reticulum (ER) or secretory pathway, and nuclear—can be used to categorize mammalian FKBPs. One PPIase domain is present in both the nuclear FKBP25 and 133 and the cytoplasmic FKBP12 and 12.6 isoforms. Multiple TPR domains are found in FKBPs 36, 38, 51, and 52. An N-terminal ER signal peptide is present in the ER FKBPs FKBP13, 19, 22, 23, 60, and 65.
| Structure | Cat No. | Product Name | CAS No. | Product Description |
|---|---|---|---|---|
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V1936 | Ascomycin (FK520) | 104987-12-4 | Ascomycin (also known as FK520, FR 900520, Immunomycin), a natural product isolated from Streptomyces, is anethyl analog of tacrolimus (FK506) anda neutral macrolide immunosuppressant, which prevents rejection after an organ transplant. |
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V33117 | S107 hydrochloride | 1357476-46-0 | S107 hydrochloride is a novel, potent and RyR-selective 1,4-benzothiazepine analogue that stabilizes RyR2 channels by enhancing the binding affinity of calstabin2 to mutant and/or PKA-phosphorylated channels. |
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