Description
Recombinant Human IL-22BP/IL-22RA2 Protein (His Tag)(Active) | PKSH033384 | Gentaur US, UK & Europe Disrtribition
Synonyms: Interleukin-22 Receptor Subunit Alpha-2; IL-22 Receptor Subunit Alpha-2; IL-22R-Alpha-2; IL-22RA2; Cytokine Receptor Class-II Member 10; Cytokine Receptor Family 2 Member 10; CRF2-10; Cytokine Receptor Family Type 2 Soluble 1; CRF2-S1; Interleukin-22-Binding Protein; IL-22BP; IL22BP; ZcytoR16; IL22RA2
Active Protein: Active protein
Activity: Recombinant Human Interleukin-22 receptor subunit alpha-2/Interleukin-22 Binding Protein is produced by our Mammalian expression system and the target gene encoding Thr22-Pro231 is expressed with a 6His tag at the C-terminus.
Protein Construction: Recombinant Human Interleukin-22 receptor subunit alpha-2/Interleukin-22 Binding Protein is produced by our Mammalian expression system and the target gene encoding Thr22-Pro231 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: 25.7 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: Interleukin-22 Receptor Subunit α-2 (IL22RA2) belongs to the type II cytokine receptor family. IL22RA2 is a secreted protein and contains three fibronectin type-III domains. IL22RA2 is widely expressed in many tissues. IL22RA2 functions as an IL22 antagonist and may be important in the regulation of inflammatory response. Three alternatively spliced transcript variants encoding distinct isoforms have been described.
Research Area: N/A
