Deinococcus grandis Single-Stranded DNA-Binding Protein (DgrSSB)

Catalog #: EG-1004
$495.00
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Product Description
Product Name Deinococcus grandis Single-Stranded DNA-Binding Protein (DgrSSB)
Overview The single-stranded DNA-binding protein from Deinococcus grandis (DgrSSB) is a thermostable, homodimeric protein essential for DNA replication, recombination, and repair in this extremophile. Each DgrSSB monomer contains two oligonucleotide/oligosaccharide-binding (OB) folds, resulting in a functional dimer with four OB domains—a structural arrangement distinctive to the Deinococcus-Thermus group. DgrSSB binds single-stranded DNA (ssDNA) with high affinity, protecting it from nucleolytic degradation and preventing secondary structure formation. It efficiently supports DNA metabolic processes and can complement the function of E. coli SSB in vivo[1][2][3][8].
Size 100 µg
Concentration 1 mg/mL
Molecular Weight ~32.3 kDa (monomer); ~64.6 kDa (homodimer functional unit)[1][2]
Key Features
  • Homodimeric structure, each monomer with two OB folds (four OB folds per dimer)[1][2][8]
  • Thermostable; half-life ~1 min at 65–67.5 °C[1][2]
  • High-affinity binding to ssDNA with a binding site size of ~33 nucleotides per dimer[1][2][3]
  • Prevents secondary structure formation and protects ssDNA from degradation
  • Functionally complements E. coli SSB in vivo[1][2]
Applications
  • Stabilization of ssDNA in high-temperature molecular biology assays
  • Studies of DNA replication, recombination, and repair in extremophiles
  • Model system for investigating unique SSB architectures and DNA-protein interactions
Source Recombinant protein expressed in E. coli[1][2]
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
  • Filipkowski, P., & Kur, J. Identification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins. Acta Biochim Pol. 2007; 54(1): 157–169.[1][2][3][8]
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