Recombinant Human TXNDC15 Protein (His Tag) | PKSH033107

Recombinant Human TXNDC15 Protein (His Tag) | PKSH033107 | Gentaur US, UK & Europe Disrtribition

Synonyms: Thioredoxin domain-containing protein 15;C5orf14;UNQ335/PRO534

Active Protein: N/A

Activity: Recombinant Human Thioredoxin Domain-Containing Protein 15 is produced by our Mammalian expression system and the target gene encoding Val33-Ser321 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Human Thioredoxin Domain-Containing Protein 15 is produced by our Mammalian expression system and the target gene encoding Val33-Ser321 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-6His

Species: Human

Expressed Host: Human Cells

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

Purity: > 95 % 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: 32.5 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH7.4.

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

Background: Thioredoxin domain-containing protein 15(TXNDC15) is a single-pass type I membrane protein. Mature Human TXNDC15 consists of a 289 amino acid (aa) extracellular region (ECD) with one thioredoxin domain, a 21 aa transmembrane domain, and a 18 aa cytoplasmic region. It has 2 isoforms produced by alternative splicing. Thioredoxins comprise a family of small proteins that, by catalyzing the oxidation of disulfide bonds, participate in redox reactions throughout the cell. Proteins that contain thioredoxin domains do not necessarily convey the oxidative properties of thioredoxins, but generally function as disulfide isomerases that enzymatically rearrange disulfide bonds found in various proteins.

Research Area: Cell biology