ULBP2 Human, Sf9
目录号 : GP24951UL16 Binding Protein 2 Human Recombinant, Sf9
Sample solution is provided at 25 µL, 10mM.
Purity | Greater than 90% as determined by SDS-PAGE. | Source | Sf9,Baculovirus cells. |
Phycical Appearance | Sterile Filtered colorless solution. | Shipping Condition | Shipped with Ice Packs. |
Synonyms | ULBP2; ALCAN-alpha; N2DL2; NKG2DL2; RAET1H; UL16 BindingProtein 2; Retinoic Acid Early Transcript 1H; UL16-Binding Protein 2;ALCAN-Alpha; NKG2D Ligand 2; N2DL-2. | ||
Amino Acid Sequence | ADPGRADPHSLCYDITVIPK FRPGPRWCAV QGQVDEKTFL HYDCGNKTVT PVSPLGKKLN VTTAWKAQNP VLREVVDILTEQLRDIQLEN YTPKEPLTLQ ARMSCEQKAE GHSSGSWQFS FDGQIFLLFD SEKRMWTTVH PGARKMKEKWENDKVVAMSF HYFSMGDCIG WLEDFLMGMD STLEPSAGAP LAMSHHHHHH. | ||
Stability | Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. | ||
Formulation | ULBP2 protein solution (0.5mg/ml) containing PhosphateBuffered Saline (pH 7.4) and 10% glycerol. |
ULBP2 is a member of the MHC class I family. ULBP2 is ligand for the NKG2D receptor, composed with at least ULBP1 and ULBP3. ULBPs promote multiple signaling pathways in primary NK cells, triggering the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D encourages calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 cooperates with soluble CMV glycoprotein UL16. This cooperation is blocked with the NKG2D receptor, providing a mechanism in which CMV infected cells can escape the immune system. Additionally, UL16 causes ULBP2 to be held in the ER and cis-Golgi apparatus so that it does not reach the cell surface.
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.