Analytical Data
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Gene name
FKBP14
- Application
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Alternative Names
FKBP14；FKBP22;Peptidyl-prolyl cis-trans isomerase FKBP14
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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
Q9NWM8
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Expression Region
20-211aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMALIPEPEVKIEVLQKPFICHRKTKGGDLM LVHYEGYLEKDGSLFHSTHKHNNGQPIWFTLGILEALKGWDQGLKGMCVG EKRKLIIPPALGYGKEGKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMD LNDDWKLSKDEVKAYLKKEFEKHGAVVNESHHDALVEDIFDKEDEDKDGF ISAREFTYKHDEL
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Molecular Weight
24 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
FKBP14 (FK506-binding protein 14) is a member of the FKBP family of proteins, which are known to function as immunophilins and peptidyl-prolyl isomerases. This protein has garnered significant research interest due to its involvement in various cellular processes, including protein folding, trafficking, and degradation. Notably, mutations in the FKBP14 gene are associated with a rare genetic disorder known as myopathy with respiratory insufficiency and cardiovascular involvement (Miyoshi myopathy), highlighting the protein's importance in muscle and cardiac function. Researchers are increasingly focusing on the structural and functional characterization of FKBP14, utilizing techniques such as X-ray crystallography and NMR spectroscopy to understand its molecular mechanisms. Furthermore, the expression of recombinant FKBP14 allows for detailed investigation of its interactions with ligands and other cellular partners, paving the way for potential therapeutic strategies targeting FKBP14-related diseases. By elucidating the roles of FKBP14 in cellular physiology and its implications in disease, scientists aim to provide deeper insights into muscle and cardiac pathologies, thereby advancing the development of targeted therapies.
