| Product Name |
Thermus thermophilus Single-Stranded DNA-Binding Protein (TthSSB) |
| Overview |
The single-stranded DNA-binding protein from Thermus thermophilus (TthSSB) is a thermostable protein that binds single-stranded DNA (ssDNA) with high affinity and specificity. TthSSB plays a critical role in DNA replication, recombination, and repair in this thermophilic bacterium. Its remarkable stability and activity at elevated temperatures make it particularly valuable for molecular biology applications that require robust ssDNA stabilization under thermal cycling or high-temperature conditions. TthSSB is structurally similar to other bacterial SSBs, functioning as a homotetramer, and is widely used to enhance the efficiency and fidelity of PCR and other DNA amplification techniques.
|
| Size |
100 µg |
| Concentration |
1 mg/mL |
| Molecular Weight |
~18.5 kDa (monomer); ~74 kDa (homotetramer) |
| Key Features |
- Thermostable: active at temperatures up to 90 °C
- Binds ssDNA with high affinity and specificity
- Prevents formation of secondary structures in ssDNA
- Facilitates high-temperature DNA replication, repair, and recombination
- Functions as a homotetramer, similar to E. coli SSB
|
| Applications |
- Thermostable DNA amplification (PCR, isothermal amplification)
- In vitro DNA replication and repair assays at high temperature
- Stabilization of ssDNA in molecular biology and biotechnology workflows
- Model system for studying DNA-protein interactions in thermophiles
|
| Source |
Recombinant protein expressed in E. coli |
| Quality Control |
- Purity >95% by SDS-PAGE
- Functional validation in ssDNA-binding assays
|
| Formulation |
20 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 10% glycerol, pH 7.5 |
| Storage |
-80 °C (long-term); avoid repeated freeze-thaw cycles |
| References |
- Yoshida, M., et al. "Purification and characterization of the single-stranded DNA binding protein from Thermus thermophilus HB8." J Biochem. 1998; 123(2): 373–379.
- Meyer, R.R., et al. "Single-stranded DNA-binding proteins: multiple forms and multiple functions." Microbiol Rev. 1990; 54(4): 342–380.
- Qing, Y., et al. "Crystal structure of the single-stranded DNA-binding protein from Thermus thermophilus HB8." J Mol Biol. 2007; 367(3): 921–929.
|