Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP8 (FKBP8)
Description
Introduction to Recombinant Human Peptidyl-prolyl cis-trans Isomerase FKBP8
Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP8 (FKBP8) is a protein produced through recombinant DNA technology. It belongs to the family of FK506 binding proteins, which are known for their peptidyl-prolyl cis-trans isomerase activity. This enzyme plays a crucial role in protein folding and has been implicated in various cellular processes, including autophagy and mitochondrial dynamics.
Production and Sources of Recombinant FKBP8
Recombinant FKBP8 can be produced in various expression systems, including yeast, E. coli, baculovirus, and mammalian cells. Each system offers different advantages in terms of yield, purity, and post-translational modifications. For example, yeast and E. coli are commonly used for large-scale production due to their high yield and cost-effectiveness, while mammalian cells provide more authentic post-translational modifications .
| Expression System | Advantages | Disadvantages |
|---|---|---|
| Yeast | High yield, cost-effective | Limited post-translational modifications |
| E. coli | High yield, cost-effective | Limited post-translational modifications |
| Baculovirus | High yield, suitable for complex proteins | Requires insect cell culture |
| Mammalian Cells | Authentic post-translational modifications | Lower yield, higher cost |
Biological Functions of FKBP8
FKBP8 is involved in several critical biological processes:
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Mitochondrial Dynamics and Autophagy: FKBP8 facilitates mitochondrial fragmentation, which is essential for mitophagy, a process by which damaged mitochondria are degraded to maintain cellular health .
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Protein Folding: As a peptidyl-prolyl cis-trans isomerase, FKBP8 helps in the proper folding of proteins, which is crucial for their function and stability.
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Interaction with Other Proteins: FKBP8 interacts with proteins like VISA, suggesting its role in signaling pathways .
Research Findings and Implications
Recent studies have highlighted the importance of FKBP8 in autophagy regulation. The absence of FKBP8 impairs autophagy activation, indicating its role as a regulatory protein in starvation-activated autophagy . Additionally, FKBP8 variants have been associated with spina bifida, suggesting its involvement in developmental processes .
Tissue Expression and Localization
FKBP8 exhibits cytoplasmic expression with a granular pattern in most cell types, as observed in human tissues. This widespread expression underscores its potential role in various cellular processes across different tissues .
Clinical and Therapeutic Potential
Given its involvement in autophagy and mitochondrial dynamics, FKBP8 may have implications for diseases related to mitochondrial dysfunction or impaired autophagy. Further research is needed to explore its therapeutic potential.
Product Specs
Note: We will prioritize shipping the format currently in stock. If you require a specific format, please specify this in your order notes; we will accommodate your request to the best of our ability.
Note: All proteins are shipped with standard blue ice packs unless otherwise requested. Dry ice shipping requires prior arrangement and incurs additional charges.
The specific tag type will be determined during production. If you require a particular tag, please inform us, and we will prioritize its development.
Target Background
Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP8 (FKBP8) is a constitutively inactive peptidyl-prolyl isomerase that becomes active upon binding to calmodulin and calcium. It functions as a chaperone for BCL2, targeting it to the mitochondria and modulating its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex likely interferes with BCL2's interaction with its targets. Therefore, the active form of FKBP8 may play a significant role in apoptosis regulation.
Relevant Research Publications:
- The dynamic interplay between Rheb and FKBP38: PMID: 29194576
- FKBP8 and Hsp90β in CLC-1 chloride channel biosynthesis: PMID: 27580824
- FKBP8 and LC3A in mitophagy induction: PMID: 28381481
- FKBP8 binding to Hsp90 and ATPase activity: PMID: 28278223
- Catalytic activity and regulation of FKBP38: PMID: 24145868
- S100P and FKBP38 interaction with Bcl-2: PMID: 24295050
- FKBP8 in CFTR folding and stability: PMID: 22474283
- Structural model of Bcl-2 and FKBP38 catalytic domain complex: PMID: 22523079
- Dual role of FKBP38 in CFTR regulation: PMID: 22030396
- PA activation of mTORC1 and FKBP38 displacement: PMID: 21737445
- Charge-sensitive site in FKBP domain regulation: PMID: 20140889
- Structural arrangement of FKBP38/calmodulin complex: PMID: 20707607
- FKBP38 and caspase-dependent degradation of Bcl-2: PMID: 20139069
- Rheb GTPase, FKBP38, Bcl-2, and Bcl-XL interaction: PMID: 20048149
- FKBP38 and TSC gene-dependent cell size regulation: PMID: 12894220
- Bcl-2 and FKBP38 interaction and phosphorylation: PMID: 15733859
- FKBP38 and calcineurin subcellular distribution: PMID: 15757646
- Molecular model of FKBP38 FK506-binding domain: PMID: 16604427
- NS5A, FKBP8, and Hsp90 in HCV RNA replication: PMID: 17024179
- FKBP38 and PHD2 protein stability: PMID: 17353276
- FKBP38 and HERG potassium channel trafficking: PMID: 17569659
- FKBP38 and 26S proteasome anchoring: PMID: 17573772
- FKBP38, calmodulin, and Bcl-2 regulation: PMID: 17942410
- FKBP38 as an endogenous inhibitor of mTOR: PMID: 17991864
- NS5A and FKBP8 interaction in HCV replication: PMID: 18216108
- FKBP38 as a Rheb effector in mTOR activation: PMID: 18658153
- TCTP and FKBP38 in mTORC1 signaling: PMID: 18676370
- FKBP38 and mTORC1 activation: PMID: 19222999
- PHD2 protein stability and FKBP38-mediated proteasomal interaction: PMID: 19546213
