Recombinant Uncharacterized protein Rv2240c/MT2300 (Rv2240c, MT2300)
Description
Introduction to Recombinant Uncharacterized Protein Rv2240c/MT2300
Recombinant Uncharacterized Protein Rv2240c/MT2300, also referred to as Rv2240c and MT2300, is a protein derived from the genetic material of Mycobacterium tuberculosis, a bacterium responsible for tuberculosis. This protein is expressed in Escherichia coli (E. coli) using recombinant DNA technology, which allows for the production of large quantities of the protein for research purposes. The protein is often tagged with a His-tag to facilitate purification and detection.
Characteristics of Recombinant Uncharacterized Protein Rv2240c/MT2300
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Source: The protein is expressed in E. coli using an in vitro expression system .
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Purity: The purity is typically greater than 90% as determined by SDS-PAGE .
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Tag: Commonly tagged with a His-tag for easy purification and identification .
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Protein Length: The full-length protein consists of 265 amino acids .
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Amino Acid Sequence: The sequence includes MGQIVAGEIGGQRTTPVGGGLPLACCLDGRPPIVPHRRRRRIAALRSVLRMRDTPRPARS RCDQVTSHAVLIGWRAVPRRHGGELPRRGALALGCIALLLMGIVGCTTVTDGTAMPDTNV APAYRSSVSASVSASAATSSIRESQRQQSLTTKAIRTSCDALAATSKDAIDKVNAYVAAF NQGRNTGPTEGPAIDALNNSASTVSGSLSAALSAQLGDALNAYVDAARAVANAIGAHAST AEFNRRVDRLNDTKTKALTMCVAAF .
Table 2: Amino Acid Sequence of Recombinant Uncharacterized Protein Rv2240c/MT2300
| Sequence |
|---|
| MGQIVAGEIGGQRTTPVGGGLPLACCLDGRPPIVPHRRRRRIAALRSVLRMRDTPRPARS RCDQVTSHAVLIGWRAVPRRHGGELPRRGALALGCIALLLMGIVGCTTVTDGTAMPDTNV APAYRSSVSASVSASAATSSIRESQRQQSLTTKAIRTSCDALAATSKDAIDKVNAYVAAF NQGRNTGPTEGPAIDALNNSASTVSGSLSAALSAQLGDALNAYVDAARAVANAIGAHAST AEFNRRVDRLNDTKTKALTMCVAAF |
Product Specs
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The tag type will be determined during the production process. If a specific tag type is required, please inform us for prioritized development.
Q&A
The following FAQs address key research considerations for working with Recombinant Uncharacterized Protein Rv2240c/MT2300 (Rv2240c, MT2300), synthesized from current literature and experimental methodologies:
Advanced Research Questions
How to resolve contradictions in structural predictions vs experimental data?
The C-terminal region (W56-D71) shows intrinsic disorder in solution ( ), conflicting with α-helix predictions. Experimental validation workflow:
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NMR spectroscopy: Map flexible regions (absent HSQC cross-peaks indicate dynamics)
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Hydrogen-deuterium exchange MS: Identify protected β-sheet regions (residues 10–40)
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Molecular dynamics simulations: Model β3:β1:β2 sheet stability (100 ns trajectories recommended)
What functional studies could elucidate its role in M. tuberculosis?
Hypothesis-driven approaches:
| Hypothesis | Method | Expected Outcome |
|---|---|---|
| Siderophore interaction | ITC with mycobactin | Kd < 10 μM supports iron metabolism role |
| Host-pathogen interaction | Yeast two-hybrid with human proteins | Identify immune evasion partners |
| Enzymatic activity | High-throughput substrate screening | Test hydrolase/transferase activity |
How to design mutagenesis studies for functional domains?
Focus on conserved regions:
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WXDXR motif (AA 56–60): Ala-scanning mutagenesis
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β-sheet interface (V12, L24, I30): Stability mutants (e.g., V12G)
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His-tag position: C-terminal vs N-terminal tagging effects on folding ( vs )
Data Discrepancy Analysis
7. Interpreting conflicting solubility reports:
Variations arise from:
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Buffer composition: 6% trehalose in storage buffer prevents aggregation ( )
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Redox state: Cys residues at 45/89 may form disulfides – test with/without TCEP
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Species differences: Human vs mycobacterial ortholog stability ( )
8. Reconciling structural models from NMR vs crystallography:
The monomeric solution structure ( ) vs potential crystal packing artifacts:
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Perform SEC-MALS for oligomerization state
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Compare 15N relaxation data (R1/R2) to crystal B-factors
