Analytical Data
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Gene name
IFT27
- Application
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Alternative Names
Putative GTP-binding protein RAY-likeRab-like protein 4
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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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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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) complex, plays a pivotal role in the assembly and maintenance of cilia and flagella, essential cellular structures involved in various physiological processes. Cilia are involved in signaling pathways and sensory functions, and disturbances in their formation or function can lead to a range of ciliopathies, including polycystic kidney disease and retinal degeneration. Recent studies have provided insights into the molecular mechanisms of IFT27, revealing its involvement in cargo transport along the axoneme and its regulatory role in IFT particle assembly. Given the essential nature of ciliary structures in cellular homeostasis and development, understanding the function and regulation of IFT27 has significant implications for identifying potential therapeutic targets for ciliopathy-related diseases. The recombinant expression of IFT27 allows for a detailed study of its biochemical properties, interactions with other IFT proteins, and the elucidation of its functional roles in ciliary dynamics. As researchers continue to decode the complexities of ciliary biology, the investigation of IFT27 and its pathways stands out as a crucial avenue for advancing our knowledge and addressing the challenges posed by ciliary disorders.
