Analytical Data
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Gene name
FKBP4
- Application
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Alternative Names
FKBP52; FKBP59; HBI; Hsp56; p52; Rotamase; 51 kDa FK506-binding protein; 59 kDa immunophilin; HSP-binding immunophilin; Peptidyl-prolyl cis-trans isomerase FKBP4
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02790
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Expression Region
Thr2~Ala459
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Molecular Weight
82kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
FKBP4 (FK506-binding protein 4) is a member of the FKBP family of proteins, known for their protein-folding and chaperone activities, and plays a crucial role in regulating various cellular processes, including signal transduction, protein stability, and transport. In recent years, FKBP4 has garnered attention due to its involvement in stress responses and its potential implications in various diseases, such as cancer and neurodegenerative disorders. The protein interacts with numerous client proteins, including steroid hormone receptors and signaling molecules, thus influencing cellular pathways crucial for homeostasis and response to external stimuli. Moreover, FKBP4's role in the assembly and disassembly of multi-protein complexes makes it an interesting target for therapeutic interventions. The study of FKBP4 recombinant proteins is essential for understanding its structure-function relationship and the mechanisms underlying its chaperone activity. This research can offer insights into developing novel strategies for modulating FKBP4 activity in disease contexts, thereby contributing to advancements in targeted therapies. Understanding the biochemical properties of FKBP4, along with its interaction networks, could pave the way for innovative approaches in drug design and biomolecular research, particularly in diseases where protein misfolding or misregulation is prevalent. Consequently, the recombinant production of FKBP4 provides a vital tool for elucidating its functional roles in cellular physiology and pathology.
