The cotransporter SGLT2 is responsible for 90% of the renal glucose reabsorption and we recently shown that MAP17 appears to work as a required beta subunit. We report in the present paper a detailed functional characterisation of human SGLT2 in co-expression with human MAP17 in Xenopus laevis oocytes. Addition of external glucose generates a large inward current in the presence of Na confirming an electrogenic transport mechanism. At a membrane potential of -50 mV, SGLT2 affinity constants for glucose and Na are 3.4 ±0.4 mM and 18 ± 6 mM, respectively. The change in the reversal potential of the cotransport current as a function of external glucose concentration clearly confirms a 1Na:1glucose transport stochiometry. SGLT2 is selective for glucose and alpha-methylglucose but it also transports, to a lower extent, galactose and 3-O-methyl-glucose. SGLT2 can be inhibited in a competitive manner by phlorizin (Pz, Ki=31 ±4 nM ) and by dapagliflozin (Ki= 0.75 ±0.3 nM). Similarly to SGLT1, SGLT2 can be activated by Na, Li and protons. Presteady-state currents for SGLT2 do exist but they are small in amplitude and relatively fast (a time constant of ~2 ms). The leak current defined as the Pz-sensitive current in the absence of substrate was extremely small in the case of SGLT2. In summary, in comparison to SGLT1, SGLT2 has a lower affinity for glucose, a transport stoichiometry of 1:1, very small pre-steady-state and leak currents, a 10 fold higher affinity for phlorizin and an affinity for dapagliflozin in the sub nM range.