Analytical Data
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Gene name
FBXO42
- Application
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Alternative Names
Fbx42; JFK; Just one F-box and Kelch domain-containing protein; F-box only protein 42
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6P3S6
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Expression Region
Gln356~Arg717
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Molecular Weight
52kDa
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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
FBXO42, a member of the F-box protein family, plays a crucial role in the ubiquitin-proteasome system, which regulates protein degradation and cellular homeostasis. This protein features a conserved F-box domain that facilitates its interaction with SKP1, a key component of the E3 ubiquitin ligase complex, allowing FBXO42 to target specific proteins for ubiquitination and subsequent degradation. Research has revealed that FBXO42 is implicated in various biological processes, including cell cycle regulation, apoptosis, and embryonic development. Abnormal expression or dysfunction of FBXO42 has been associated with various diseases, including cancer, where it may influence tumor progression by modulating the degradation of oncogenic or tumor suppressor proteins. The study of FBXO42, particularly its recombinant protein, provides valuable insights into its functional mechanisms and potential as a therapeutic target. Understanding the structure and function of the recombinant FBXO42 protein could lead to the identification of novel intervention strategies for diseases linked to its dysregulation, thus emphasizing its significance in both fundamental biology and clinical research.
