FKBP1A Mouse
Description
FKBP1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
FKBP1A is a 12kDa protein initially discovered on immune cells based on its ability to bind and mediate the intracellular effects of the immunosuppressant FK506. FKBP1A is also known to mediate the action of Rapamycin, an immunosuppressive agent. FKBP1A belongs to the immunophilin family, characterized by their high affinity for immunosuppressant drugs and their peptidyl-prolyl cis-trans isomerase (PPIase) activity, which participates in folding proteins containing proline. In the absence of immunosuppressive ligands, FKBP1A is involved in intracellular calcium regulation by associating with three types of Ca2+ release channel complexes: skeletal ryanodine receptors, cardiac ryanodine receptors, and the inositol 1,4,5-triphosphate receptor. FKBP1A also interacts with the TGF-beta type I receptor, inhibiting the TGF-beta signaling pathway. FKBP12 modulates ryanodine receptor isoform-1 (ryr-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. FKBP1A enhances protein folding and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Product Science Overview
FK506 Binding Protein 1A (FKBP1A), also known as FKBP12, is a member of the immunophilin protein family. These proteins are known for their ability to bind immunosuppressive drugs such as FK506 (tacrolimus) and rapamycin . FKBP1A is a highly conserved protein found in various species, including mice, where it plays a crucial role in several cellular processes.
The discovery of FKBP1A dates back to the 1970s when researchers were investigating the molecular mechanisms of immunosuppressive drugs. FK506, a potent immunosuppressant, was isolated from the bacterium Streptomyces tsukubaensis. Subsequent studies identified FKBP1A as the cytosolic receptor for FK506 . The protein was initially purified from bovine thymus, human spleen, and Jurkat T-cell lines .
FKBP1A is a small protein with a molecular weight of approximately 12 kDa. It contains a highly conserved domain known as the FK-12-like domain, which is responsible for its peptidyl-prolyl isomerase (PPIase) activity . This activity allows FKBP1A to catalyze the cis-trans isomerization of proline residues in peptide bonds, which is crucial for protein folding and function.
In addition to its PPIase activity, FKBP1A acts as a co-receptor for FK506 and rapamycin. When bound to FK506, FKBP1A forms a complex with calcineurin, inhibiting its phosphatase activity and leading to immunosuppression . Similarly, the FKBP1A-rapamycin complex inhibits the mechanistic target of rapamycin (mTOR) pathway, affecting cell growth and proliferation .
FKBP1A is involved in various cellular processes, including:
- Protein Folding: FKBP1A assists in the proper folding of newly synthesized proteins by catalyzing the cis-trans isomerization of proline residues .
- Signal Transduction: By forming complexes with FK506 and rapamycin, FKBP1A regulates key signaling pathways such as calcineurin and mTOR .
- Calcium Homeostasis: FKBP1A interacts with ryanodine receptors, which are involved in calcium release from the endoplasmic reticulum, thus playing a role in calcium signaling .
The study of FKBP1A has significant implications for both basic research and therapeutic applications. Understanding the molecular mechanisms of FKBP1A can provide insights into the regulation of immune responses and the development of immunosuppressive therapies. Additionally, FKBP1A is a potential target for drug development in diseases related to protein misfolding and dysregulated signaling pathways .
