Analytical Data
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Gene name
WDFY3
- Application
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Alternative Names
WDFY3; KIAA0993; WD repeat and FYVE domain-containing Protein 3; Autophagy-linked FYVE Protein; Alfy
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IZQ1
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Expression Region
1-420 aa
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AA Sequence
MGTSKEKAKTATLKQALLGHTDTVTCATASLAYHIIVSGSRDRTCIIWDLNKLSFLTQLRGHRAPVSALCINELTGDIVSCAGTYIHVWSINGNPIVSVNTFTGRSQQIICCCMSEMNEWDTQNVIVTGHSDGVVRFWRMEFLQVPETPAPEPAEVLEMQEDCPEAQIGQEAQDEDSSDSEADEQSISQDPKDTPSQPSSTSHRPRAASCRATAAWCTDSGSDDSRRWSDQLSLDEKDGFIFVNYSEGQTRAHLQGPLSHPHPNPIEVRNYSRLKPGYRWERQLVFRSKLTMHTAFDRKDNAHPAEVTALGISKDHSRILVGDSRGRVFSWSVSDQPGRSAADHWVKDEGGDSCSGCSVRFSLTERRHHCRNCGQLFCQKCSRFQSEIKRLKISSPVRVCQNCYYNLQHERGSEDGPRNC
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Molecular Weight
71.94 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
WDFY3, or WD repeat and FYVE domain-containing protein 3, is a multifunctional protein that plays a crucial role in various cellular processes, including autophagy, endocytosis, and immune response regulation. The study of WDFY3 has gained attention due to its involvement in several diseases, particularly those related to immune dysfunction and cellular signaling pathways. Mutations and dysregulation of WDFY3 have been linked to immunological disorders and potentially contribute to cancer progression. Researchers have focused on characterizing WDFY3's structural properties using recombinant protein techniques to elucidate its biological functions and interactions with other cellular molecules. By expressing WDFY3 as a recombinant protein, scientists can conduct in-depth biochemical analyses, identify binding partners, and define the specific roles it plays within the cell. This understanding could pave the way for developing therapeutic strategies targeting WDFY3-associated pathways, offering hope for the treatment of related diseases. The investigation of WDFY3 as a recombinant protein is thus of significant scientific interest, providing insights into its function and relevance in human health.
