Analytical Data
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Gene name
FKBP2
- Application
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Alternative Names
FKBP2；FKBP13FKBP9;Peptidyl-prolyl cis-trans isomerase FKBP2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P26885
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Expression Region
22-142aa
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AA Sequence
ATGAEGKRKLQIGVKKRVDHCPIKSRKGDVLHMHYTGKLEDGTEFDSSLP QNQPFVFSLGTGQVIKGWDQGLLGMCEGEKRKLVIPSELGYGERGAPPKI PGGATLVFEVELLKIERRTELVDHHHHHH
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Molecular Weight
14 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
FKBP2 (FK506-binding protein 2) is a member of the immunophilin family, known for its role in protein folding and trafficking, as well as intracellular signaling in response to stress. This protein exhibits peptidyl-prolyl isomerase activity, which is crucial for protein conformational changes and is implicated in various cell processes, including apoptosis and inflammation. Aberrant expression of FKBP2 has been linked to several diseases, including cancer and neurodegenerative disorders, making it a significant target for therapeutic interventions. Recent advances in recombinant protein technology have enabled the production and characterization of FKBP2 for further study. By generating recombinant FKBP2, researchers aim to elucidate its structure-function relationships, identify potential binding partners, and explore its role in pathological conditions. The study of FKBP2 not only provides insights into cellular mechanisms but also contributes to the development of novel therapeutic strategies targeting FKBP2-related pathways, highlighting its potential as a biomarker and therapeutic target in various diseases. Thus, understanding FKBP2 through recombinant technologies can pave the way for innovative approaches in disease management and treatment.
