Potassium-transporting ATPase alpha chain 1 (ATP4A), partial, human, recombinant

Organism: Homo sapiens (Human). Source: E.coli. Expression Region: 350-783aa. Protein Length: Partial. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: TVTVCLSLTA KRLASKNCVV KNLEAVETLG STSVICSDKT GTLTQNRMTV SHLWFDNHIH TADTTEDQSG QTFDQSSETW RALCRVLTLC NRAAFKSGQD AVPVPKRIVI GDASETALLK FSELTLGNAM GYRDRFPKVC EIPFNSTNKF QLSIHTLEDP RDPRHLLVMK GAPERVLERC SSILIKGQEL PLDEQWREAF QTAYLSLGGL GERVLGFCQL YLNEKDYPPG YAFDVEAMNF PSSGLCFAGL VSMIDPPRAT VPDAVLKCRT AGIRVIMVTG DHPITAKAIA ASVGIISEGS ETVEDIAARL RVPVDQVNRK DARACVINGM QLKDMDPSEL VEALRTHPEM VFARTSPQQK LVIVESCQRL GAIVAVTGDG VNDSPALKKA DIGVAMGIAG SDAAKNAADM ILLDDNFASI VTGVEQGRLI FDNL. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: The catalytic subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H(+) ions to the gastric lumen while transporting K(+) ion from the lumen into the cell. Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1. Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H(+) ion in the stomach lumen is followed by binding of K(+) ion converting the pump conformation back to the E1 state. Reference: "Modulation of H(+),K(+)-ATPase activity by the molecular chaperone ERp57 highly expressed in gastric parietal cells." Fujii T., Awaka S.Y., Takahashi Y., Fujita K., Tsuji H., Shimizu T., Gomi T., Tsukada K., Sakai H. FEBS Lett. 587:3898-3905(2013). Function: nan