Analytical Data
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Gene name
FBXL14
- Application
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Alternative Names
FBXL14; FBL14F-box/LRR-repeat protein 14; F-box and leucine-rich repeat protein 14
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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
Q8N1E6
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Expression Region
1-418aa
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AA Sequence
METHISCLFPELLAMIFGYLDVRDKGRAAQVCTAWRDAAYHKSVWRGVEAKLHLRRANPSLFPSLQARGIRRVQILSLRRSLSYVIQGMANIESLNLSGCYNLTDNGLGHAFVQEIGSLRALNLSLCKQITDSSLGRIAQYLKGLEVLELGGCSNITNTGLLLIAWGLQRLKSLNLRSCRHLSDVGIGHLAGMTRSAAEGCLGLEQLTLQDCQKLTDLSLKHISRGLTGLRLLNLSFCGGISDAGLLHLSHMGSLRSLNLRSCDNISDTGIMHLAMGSLRLSGLDVSFCDKVGDQSLAYIAQGLDGLKSLSLCSCHISDDGINRMVRQMHGLRTLNIGQCVRITDKGLELIAEHLSQLTGIDLYGCTRITKRGLERITQLPCLKVLNLGLWQMTDSEKEARGDFSPLFTVRTRGSSRR
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Molecular Weight
72.3 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
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Protein Description
FBXL14, a member of the F-box protein family, has garnered attention in recent years due to its role in regulating various cellular processes, including cell cycle progression, differentiation, and the immune response. Its function as an E3 ubiquitin ligase positions it at a crucial intersection in the ubiquitin-proteasome pathway, where it tags proteins for degradation, thus influencing protein levels and activity within the cell. Dysregulation of FBXL14 has been implicated in several diseases, including cancer, highlighting its potential as a therapeutic target. Recent studies have focused on the characterization of FBXL14, aiming at understanding its structural features, substrate interactions, and the signaling pathways it influences. The production of recombinant FBXL14 protein has become essential for these studies, allowing researchers to elucidate its biochemical properties and interactions in vitro. Moreover, understanding the precise mechanisms through which FBXL14 operates could lead to novel strategies for modulating its activity in pathological conditions. As interest in the therapeutic manipulation of the ubiquitin-proteasome system grows, FBXL14 stands out as a promising candidate for further investigation into its role in health and disease.
