Recombinant Human OBFC1/STN1 Protein (His Tag) | PKSH032832

Recombinant Human OBFC1/STN1 Protein (His Tag) | PKSH032832 | Gentaur US, UK & Europe Disrtribition

Synonyms: CST Complex Subunit STN1; Oligonucleotide/Oligosaccharide-Binding Fold-Containing Protein 1; Suppressor of Cdc Thirteen Homolog; OBFC1; STN1

Active Protein: N/A

Activity: Recombinant Human Oligosaccharide-Binding Fold-Containing Protein 1 is produced by our E.coli expression system and the target gene encoding Met1-Phe368 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Human Oligosaccharide-Binding Fold-Containing Protein 1 is produced by our E.coli expression system and the target gene encoding Met1-Phe368 is expressed with a 6His tag at the N-terminus.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 85 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 44.2 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM Tris, 1mM DTT, pH 8.0.

Reconstitution: Please refer to the printed manual for detailed information.

Background: CST Complex Subunit STN1 (OBFC1) is a 368 amino acid protein that contains one OB DNA-binding domain. It is a member of the STN1 family. OBFC1 is component of the CST complex, a complex that binds to single-stranded DNA and is required to protect telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity by themselves. In addition to telomere protection, the CST complex has probably a more general role in DNA metabolism at non-telomeric sites.

Research Area: epigenetics and nuclear signal