Analytical Data
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Gene name
FBXL2
- Application
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Alternative Names
FBXL2；FBL2；FBL3；F-box/LRR-repeat Protein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UKC9
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Expression Region
1-423aa
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AA Sequence
MVFSNNDEGLINKKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRIDLFNFQTDVEGRVVENISKRCGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSITNSSLKGISEGCRNLEYLNLSWCDQITKDGIEALVRGCRGLKALLLRGCTQLEDEALKHIQNYCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSNLTDASLTALGLNCPRLQILEAARCSHLTDAGFTLLARNCHELEKMDLEECILITDSTLIQLSIHCPKLQALSLSHCELITDDGILHLSNSTCGHERLRVLELDNCLLITDVALEHLENCRGLERLELYDCQQVTRAGIKRMRAQLPHVKVHAYFAPVTPPTAVAGSGQRLCRCCVIL
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Molecular Weight
48.3 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
FBXL2, a member of the F-box protein family, plays a crucial role in regulating various cellular processes, including cell cycle progression and protein degradation via the ubiquitin-proteasome system. Research into FBXL2 has gained significant attention due to its involvement in multiple signaling pathways and potential impact on cancer biology, where its function might influence tumor growth and metastasis. Mutations or dysregulation of FBXL2 have been implicated in several diseases, making it a valuable target for therapeutic intervention. Understanding the structure and function of FBXL2 is essential for elucidating its biological roles and developing strategies to modulate its activity. The use of recombinant protein technology has enabled researchers to produce and study FBXL2 in vitro, facilitating investigations into its interactions with substrates and other cellular partners. By characterizing the molecular mechanisms underlying FBXL2 function, this research aims to provide insights into its potential as a biomarker for disease and a target for novel treatments. As such, the study of FBXL2 recombinant protein could pave the way for innovative therapeutic strategies in cancer and other conditions linked to its dysregulation.
