Analytical Data
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Gene name
FKBPL
- Application
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Alternative Names
FKBPL；DIR1；NG7;FK506-binding Protein-like
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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
Q9UIM3
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Expression Region
1-349aa
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AA Sequence
METPPVNTIG EKDTSQPQQE WEKNLRENLD SVIQIRQQPR DPPTETLELE VSPDPASQIL EHTQGAEKLV AELEGDSHKS HGSTSQMPEA LQASDLWYCP DGSFVKKIVI RGHGLDKPKL GSCCRVLALG FPFGSGPPEG WTELTMGVGP WREETWGELI EKCLESMCQG EEAELQLPGH SGPPVRLTLA SFTQGRDSWE LETSEKEALA REERARGTEL FRAGNPEGAA RCYGRALRLL LTLPPPGPPE RTVLHANLAA CQLLLGQPQL AAQSCDRVLE REPGHLKALY RRGVAQAALG NLEKATADLK KVLAIDPKNR AAQEELGKVV IQGKNQDAGL AQGLRKMFGL EHHHHHH
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Molecular Weight
39 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
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Protein Description
FKBPL (FK506-binding protein-like) is a member of the immunophilin family, which has garnered interest due to its potential roles in cellular processes, including immune response modulation, angiogenesis, and cancer progression. Research has shown that FKBPL is involved in various signaling pathways and may exhibit tumor-suppressive properties. It is believed to interact with key proteins in the cell, influencing their function and localization. Given its impact on angiogenesis and tumor immune microenvironments, FKBPL is a candidate for therapeutic interventions in cancer treatment. Recent studies have focused on the development of FKBPL recombinant proteins to investigate their structural and functional properties, offering insights into the protein's biological mechanisms. These recombinant proteins enable researchers to explore the therapeutic potential of FKBPL in targeted cancer therapies and enhance our understanding of its role in disease progression. By generating and characterizing FKBPL in different cellular contexts, researchers aim to capitalize on its properties for novel treatment strategies against various malignancies.
