Amino acid sequence:
MPAGVGNASGSVLDMTSVRTVPSAVALVTFAGAALSGVIPAIARADPVGHQVTYTVTTTSDLMANIRYMSADPPSMAAFNADSSKYMITLHTPIAGGQPLVYTATLANPSQWAIVTASGGLRVNPEFHCEIVVDGQVVVSQDGGSGVQCSTRPW (154 residues)
Domains: No conserved domains identified in public databases.
Orthologs: Limited homology to uncharacterized proteins in Mycobacterium tuberculosis and other actinobacteria.
Proteins in the same COG (Clusters of Orthologous Groups) category as Mb2606c are often linked to RNA modification or ribosomal assembly (e.g., rRNA methyltransferases, tRNA synthetases) .
No direct experimental evidence links Mb2606c to enzymatic activity or pathway involvement .
Expression: Induced in E. coli under T7/lac promoter systems, similar to methods for other mycobacterial proteins .
Purification: Immobilized metal affinity chromatography (IMAC) for His-tag isolation .
Stability: Lyophilized powder stable at -80°C; working aliquots retain integrity for one week at 4°C .
Endotoxin levels: Not explicitly stated but typically <1 EU/μg for E. coli-derived proteins .
Batch consistency: Confirmed via mass spectrometry and N-terminal sequencing in commercial lots .
Antigen production: Used in ELISA and antibody generation due to its immunogenic properties .
Structural studies: Potential candidate for X-ray crystallography or cryo-EM due to solubility in Tris/PBS buffers .
No direct links to vaccine development or drug targeting, though uncharacterized mycobacterial proteins are often screened for host-pathogen interaction studies .
| Feature | Mb2606c | M. tuberculosis Rv2606c |
|---|---|---|
| Length | 154 aa | 153 aa |
| Sequence identity | 98% | 100% (ortholog) |
| Known function | Uncharacterized | Uncharacterized |
| Commercial availability | Yes (Creative BioMart, MyBioSource) | Limited |
Functional elucidation: High-throughput mutagenesis or CRISPR interference (CRISPRi) could identify phenotypic changes in M. bovis knockout strains .
Interaction mapping: Yeast two-hybrid screens or affinity purification mass spectrometry (AP-MS) may reveal binding partners .
Structural resolution: Cryo-EM studies could clarify its role in mycobacterial physiology .