FBXO2 Human
Description
FBXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
F-Box Protein 2 (FBXO2) is a member of the F-box protein family, which is characterized by the presence of an F-box motif. This motif is approximately 50 amino acids long and is crucial for protein-protein interactions. F-box proteins are integral components of the SCF (SKP1-CUL1-F-box protein) complex, a type of E3 ubiquitin ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins .
FBXO2, like other F-box proteins, contains an F-box domain that interacts with SKP1, a core component of the SCF complex. Additionally, FBXO2 has other protein-protein interaction motifs, such as leucine-rich repeats (LRRs), which are involved in substrate recognition . The primary function of FBXO2 is to target specific proteins for ubiquitination, thereby regulating various cellular processes, including cell cycle progression, signal transduction, and transcription .
FBXO2 plays a significant role in maintaining cellular homeostasis by regulating the degradation of misfolded glycoproteins in the endoplasmic reticulum (ER). This process is crucial for preventing the accumulation of potentially toxic proteins that can lead to cellular stress and disease . In addition, FBXO2 has been implicated in various pathological conditions, including neurodegenerative diseases and cancer .
The recombinant production of FBXO2 involves cloning the FBXO2 gene into an appropriate expression vector, followed by transformation into a suitable host cell, such as Escherichia coli or mammalian cells. The expressed protein is then purified using affinity chromatography techniques, such as nickel-nitrilotriacetic acid (Ni-NTA) chromatography, which exploits the histidine tags commonly added to recombinant proteins for purification purposes .
FBXO2, as part of the SCF complex, facilitates the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the substrate protein. This ubiquitination process involves a cascade of enzymatic reactions, starting with the activation of ubiquitin by an E1 ubiquitin-activating enzyme, followed by its transfer to an E2 enzyme, and finally to the substrate protein via the E3 ligase activity of the SCF complex . The ubiquitinated proteins are then recognized and degraded by the 26S proteasome, a large protease complex responsible for protein turnover in cells .
