Aquaporin-5 (AQP5), human, recombinant

Organism: Homo sapiens (Human). Source: in vitro E.coli expression system. Expression Region: 1-265aa. Protein Length: Full Length. Tag Info: N-terminal 10xHis-tagged. Target Protein Sequence: MKKEVCSVAF LKAVFAEFLA TLIFVFFGLG SALKWPSALP TILQIALAFG LAIGTLAQAL GPVSGGHINP AITLALLVGN QISLLRAFFY VAAQLVGAIA GAGILYGVAP LNARGNLAVN ALNNNTTQGQ AMVVELILTF QLALCIFAST DSRRTSPVGS PALSIGLSVT LGHLVGIYFT GCSMNPARSF GPAVVMNRFS PAHWVFWVGP IVGAVLAAIL YFYLLFPNSL SLSERVAIIK GTYEPDEDWE EQREERKKTM ELTTR. 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: Forms a water-specific channel . Plays an important role in fluid secretion in salivary glands. Required for TRPV4 activation by hypotonicity. Together with TRPV4, controls regulatory volume decrease in salivary epithelial cells . Seems to play a redundant role in water transport in the eye, lung and in sweat glands. Reference: "High-resolution X-ray structure of human aquaporin 5." Horsefield R., Norden K., Fellert M., Backmark A., Tornroth-Horsefield S., Terwisscha van Scheltinga A.C., Kvassman J., Kjellbom P., Johanson U., Neutze R. Proc. Natl. Acad. Sci. U.S.A. 105:13327-13332(2008). Function: nan