Analytical Data
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Gene name
FBXL22
- Application
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Alternative Names
FBXL22F-box and leucine-rich protein 22
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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
Q6P050
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Expression Region
1-241aa
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AA Sequence
MHITQLNRECLLHLFSFLDKDSRKSLARTCSQLHDVFEDPALWSLLHFRSLTELQKDNFLLGPALRSLSICWHSSRVQVCSIEDWLKSAFQRSICSRHESLVNDFLLRVCDRLSAVRSPRRREAPAPSSGTPIAVGPKSPRWGGPDHSEFADLRSGVTGARAAARRGLGSLRAERPSETPPAPGVSWGPPPPGAPVVISVKQEEGKQGRTGRRSHRAAPPCGFARTRVCPPTFPGADAFPQ
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Molecular Weight
52.91 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
FBXL22, a member of the F-box protein family, plays a crucial role in the ubiquitin-proteasome pathway, which is essential for regulating protein degradation and various cellular processes. Research into FBXL22 has gained traction due to its involvement in modulating the stability of key regulatory proteins that influence significant biological functions, such as cell cycle progression, apoptosis, and stress responses. Studies have identified FBXL22 as a potential player in several diseases, including cancer. Given its regulatory potential, understanding the structural and functional properties of FBXL22, particularly in the context of its interactions with specific substrates and E3 ligases, is vital for elucidating its role in cellular homeostasis. Recombinant FBXL22 protein provides an invaluable tool for studying its biochemical properties and functional mechanisms, enabling researchers to investigate its substrate specificity, binding affinities, and post-translational modifications. Such investigations could uncover novel therapeutic targets or strategies for diseases associated with dysregulation of protein degradation pathways. Consequently, the research surrounding FBXL22 recombinant protein not only fosters a deeper comprehension of its biological roles but also opens avenues for potential interventions in related pathological conditions.
