BCE_4008 is a recombinant protein derived from Bacillus cereus (strain ATCC 10987 / NRS 248) and belongs to the UPF0223 family of uncharacterized proteins. Key features include:
| Parameter | Details |
|---|---|
| Product Code | CSB-EP744713BQN |
| Source | E. coli expression system |
| Purity | >85% (SDS-PAGE) |
| Sequence | MEYQYPLDYD WSNEEMVTIV KFYEAIEKAY EKGIVREELM GLYRRFKEIV PSKAEEKKID KEFQEVSGYS IYRAIQKAKE IEEEKLVKM |
| Tag Info | Determined during manufacturing; not explicitly stated |
| Protein Length | Full-length (1–89 amino acids) |
The protein is provided in lyophilized or liquid form, with reconstitution recommended in deionized sterile water at 0.1–1.0 mg/mL. Glycerol (5–50% final concentration) is advised for long-term stability .
BCE_4008 is annotated as a UPF0223 protein, a family with limited functional annotation. While the exact role of UPF0223 proteins remains unclear, their presence in diverse bacterial species suggests conserved biological functions. The protein’s sequence includes hydrophobic and charged regions, indicating potential membrane association or interaction with other macromolecules.
Though direct studies on BCE_4008 are lacking, UPF0223 family members in other organisms may participate in:
Metabolic regulation: Based on B. cereus’ preference for proteinaceous substrates .
Stress response: Analogous to B. cereus’ survival mechanisms under acidic or oxidative stress .
Viral interactions: Hypothetical role in phage defense or horizontal gene transfer, given *B. cereus_’ genomic plasticity .
BCE_4008 serves as a tool in:
Structural Biology: Crystallization studies to elucidate UPF0223 family folding.
Functional Screens: Biochemical assays to identify enzymatic or binding activities.
Pathogenicity Studies: Assessing interactions with host cells or toxins in B. cereus infection models .
Functional Elucidation: No published studies directly link BCE_4008 to enzymatic activity or virulence.
Interoperability: Limited cross-referencing with other UPF0223 proteins due to sparse literature.
Post-Translational Modifications: Potential glycosylation or phosphorylation sites remain uncharacterized.