FBXO6 is fused to a 23 amino acid His-tag at N-terminus
& purified by proprietary chromatographic techniques.
Recombinant FBXO6 protein, of human origin, has been produced in an E. coli expression system. This results in a single polypeptide chain consisting of 316 amino acids (residues 1-293) with a molecular weight of 36.3 kDa.
The FBXO6 protein has been engineered to include a 23 amino acid His-tag at the N-terminus to facilitate purification using proprietary chromatographic methods.
MGSSHHHHHH SSGLVPRGSH MGSMDAPHSK AALDSINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL
IDLMTLWKRK CLREGFITKD WDQPVADWKI FYFLRSLHRN LLRNPCAEED MFAWQIDFNG GDRWKVESLP
GAHGTDFPDP KVKKYFVTSY EMCLKSQLVD LVAEGYWEEL
LDTFRPDIVV KDWFAARADC GCTYQLKVQL ASADYFVLAS FEPPPVTIQQ
WNNATWTEVS YTFSDYPRGV RYILFQHGGR DTQYWAGWYG PRVTNSSIVV SPKMTRNQAS SEAQPGQKHG
QEEAAQSPYR AVVQIF.
FBXL6 contains leucine-rich repeats (LRRs) that are involved in protein-protein interactions . The primary role of FBXL6 is to act as a substrate-recognition component of the SCF-type E3 ubiquitin ligase complex . This complex is crucial for targeting specific proteins for ubiquitination and subsequent proteasomal degradation, thereby regulating various cellular processes .
Recombinant Human FBXL6 is typically produced using an in vitro wheat germ expression system . This method helps preserve the correct conformational folding necessary for the protein’s biological function . The recombinant protein often includes a GST tag at the N-terminal, which aids in purification and detection .
Recombinant FBXL6 is used in various applications, including: