Analytical Data
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Gene name
FKBP3
- Application
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Alternative Names
25KDA FK506-binding protein ;25KDA FKBP ;FKBP-25FK506-binding protein 3 ;FKBP-3Immunophilin FKBP25Rapamycin-selective 25KDA immunophilinRotamase
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00688
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Expression Region
2-224aa
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Molecular Weight
41 kDa
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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
Related Products
Protein Description
FKBP3 (FK506-binding protein 3) is a member of the FKBP family of proteins, known for their role in immunophilin functions and as peptidyl-prolyl isomerases. Research into FKBP3 has gained momentum due to its involvement in key cellular processes such as apoptosis, protein folding, and immune response modulation. The protein has been implicated in various diseases, including cancer and neurodegenerative disorders, making it a potential biomarker and therapeutic target. Understanding the structure and function of FKBP3 is critical for elucidating its role in these pathological conditions. Recent advances in recombinant protein technology have enabled the production and characterization of FKBP3, allowing researchers to investigate its interaction with small molecules and other proteins. This research is pivotal not only for developing novel therapeutic strategies but also for enhancing our comprehension of the biochemical pathways associated with FKBP3, facilitating drug design and discovery. Through studies focused on FKBP3’s molecular mechanisms and functions, there is significant potential to uncover new insights that could lead to innovative treatments for related diseases.
