Analytical Data
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Gene name
IFT27
- Application
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Alternative Names
IFT27；RABL4；RAYL；Intraflagellar transport Protein 27 homolog
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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
Q9BW83
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Expression Region
1-186aa
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AA Sequence
MVKLAAKCILAGDPAVGKTALAQIFRSDGAHFQKSYTLTTGMDLVVKTVPVPDTGDSVELFIFDSAGKELFSEMLDKLWESPNVLCLVYDVTNEESFNNCSKWLEKARSQAPGISLPGVLVGNKTDLAGRRAVDSAEARAWALGQGLECFETSVKEMENFEAPFHCLAKQFHQLYREKVEVFRALA
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Molecular Weight
36.5 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
IFT27, a member of the intraflagellar transport (IFT) protein complex, plays a crucial role in the development and maintenance of cilia, which are essential for various cellular processes, including signal transduction and fluid movement. Cilia are hair-like structures on the surface of cells that have been implicated in various biological functions and are central to the development of many organisms. Dysfunction in ciliary proteins, including IFT27, has been linked to a range of disorders, including ciliopathies, which can cause developmental abnormalities and diseases such as Bardet-Biedl syndrome and polycystic kidney disease. Understanding the structure and function of IFT27 is vital to unraveling the mechanisms underlying cilia-related diseases. Recent studies have focused on the molecular interactions and pathways involving IFT27, aiming to elucidate its specific role in ciliary assembly and maintenance. Research into IFT27's recombinant protein is also significant for potential therapeutic applications, as it could contribute to the development of targeted treatments for ciliopathies. By exploring the biochemical properties and interactions of IFT27, scientists hope to gain insights into how ciliary transport mechanisms can be modulated, ultimately improving our understanding of ciliary biology and its implications in health and disease.
