Analytical Data
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Gene name
FIL1d
- Application
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Alternative Names
FIL1d;FIL1D;IL1F5;IL1HY1;Interleukin-36 receptor antagonist Protein
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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
Q9UBH0
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Expression Region
2-155aa
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AA Sequence
VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAGKVIKGEE ISVVPNRWLD ASLSPVILGV QGGSQCLSCG VGQEPTLTLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTVPEADQPV RLTQLPENGG WNAPITDFYF QQCD
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Molecular Weight
16.8 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
FIL1d, a member of the Filamins protein family, plays a crucial role in cell structure and signaling by linking the actin cytoskeleton to various signaling pathways. These protein complexes are essential for maintaining cellular integrity and facilitating cellular responses to environmental cues. The study of FIL1d has gained significant attention due to its involvement in several physiological processes, including cell migration, adhesion, and the regulation of cellular shape. Furthermore, alterations in FIL1d expression or function have been associated with various pathological conditions, such as cancer metastasis and cardiovascular diseases. Recent research has focused on the re-engineering of FIL1d as a recombinant protein for advanced therapeutic applications and to elucidate its molecular mechanisms. Understanding the structural and functional dynamics of FIL1d can provide insights into its role in health and disease, making it a target of interest for drug development and biomarker discovery. The ability to manipulate FIL1d through recombinant techniques presents opportunities to explore its potential in regenerative medicine and targeted therapies, offering promise for innovative treatments.











