MVFTQAPAEIMGHLRIRSLLARQCLAEFLGVFVLMLLTQGAVAQAVTSGETKGNFFTMFLAGSLAVTIAIYVGGNVSGAHLNPAFSLAMCIVGRLPWVKLPIYILVQLLSAFCASGATYVLYHDALQNYTGGNLTVTGPKETASIFATYPAPYLSLNNGFLDQVLGTGMLIVGLLAILDRRNKGVPAGLEPVVVGMLILALGLSMGANCGIPLNPARDLGPRLFTYVAGWGPEVFSAGNGWWWVPVVAPLVGATVGTATYQLLVALHHPEGPEPAQDLVSAQHKASELETPASAQMLECKL
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Water channel that mediates water transport across cell membranes irrespective of the cytosolic pH. The channel is permeable to glycerol, especially when the cytosolic pH is acidified. Contributes to adipocyte water and glycerol permeability, and may thereby contribute to the utilization of glycerol derived from phospholipid degradation. May contribute to water transport in the intestine (Probable).; Water channel that mediates water transport across cell membranes, but that is not permeable to glycerol.
Gene References into Functions
Expression of CXCL4 and aquaporin 3 and 10 mRNAs in middle ear effusion is associated with the pathophysiology of otitis media with effusion.PMID:26810286
the human aquaglyceroporins, i.e., AQP3, AQP7, AQP9 and AQP10 can act as silicon transporters in both Xenopus laevis oocytes and HEK-293 cells.PMID:26313002
Aquaporin-10 is expressed exclusively in the adipocytes, which is particularly important for the maintenance of normal or low glycerol contents inside the adipocyte, thus protecting humans from obesity.PMID:23382902
the presence of at least one glycosylated protein within each tetramer is sufficient to convey an enhanced structural stability to the remaining hAQP10 protomers of the tetramer.PMID:21733844
study unveiled the uniquely dual functional characteristic of hAQP10 as a carrier/channel for solute transport, providing a novel insight into its operation mechanism, which would help further elucidate its physiological rolePMID:21691092
Results suggest that AQP10 represents a new member of aquaglyceroporins functionally as well as structurally.PMID:12084581
AQP10 with an insertion of 475 nt was localized in the capillary endothelium in villi of the small intestine and the isoform without the insertion localized in the gastro-entero-pancrestic endocrine cells.PMID:15898950
differential polarity and selective targeting of AQP3 and AQP10 in the intestinal epithelial cells is influenced by amino acid signal motifs.PMID:18678926
Detected in epithelial cells on villi in the ileum, and also in stomach, jejunum, colon, rectum, white adipose tissue and placenta (at protein level). Expressed in duodenum and jejunum. Highest expression in absorptive epithelial cells at the tips of vill