Calcium plays a key role in the functions white fat adipocytes (WFA). Recently we verified the existence of L-type calcium voltage-gated channels (CaVs) in WFA, (Fedorenko et al., 2019a, 2019b); however, their ion channel properties remain unknown. We have used recombinant expression cloning of the identified transcriptomic sequence to biophysically and pharmacologically characterise the CaV1.2 variant expressed in WFA. Rat visceral WFA has the cacna1c gene with transcription variant x3 (accession number XM_006237175.3); interestingly, this gene encodes a unique CaV1.2 sequence with an extension between exons 9 and 10. This variation was confirmed by PCR with exon-specific primers in comparison with cDNA generated from RNAs extracted from heart and brain samples of adult male rat. To study the electrophysiological and pharmacological properties of the adipocyte CaV1.2, the sequence of the cacna1c gene, obtained from RNA sequencing of visceral WFA of male rats, was cloned into a vector construct and expressed in CHO cells. The characteristics of L-type Ba2+ and Ca2+ inward currents of CaV1.2 were determined with the whole-cell patch-clamp method and were compared with currents carried by brain-type CaV1.2. When no differences were observed between adipocyte and brain CaV1.2, data is given just for adipocytes as mean (95% confidence intervals; number of determinations). Currents were observed when CaV1.2 α1 subunit was expressed alone or was co-expressed with β and α2δ subunits (co-transfection of cacna1c, cacna2d1 and cacnab3 genes at 1:1:1 ratio); as co-transfection increased the current density ~10 fold, co-expression was used throughout this study. The kinetics of the currents in Ba2+ (IBa) or Ca2+ solutions were similar, with activation and inactivation time constants of 6.2 ms (4 to 8.3; n=8) and 322 ms (158 to 486; n=8) respectively at 10mV in 10 mM Ba2+, the half maximal voltage for IBa activation was -6.5 mV (-11 to -1.6; n=8) (n=8); values typical for CaV1.2 channels (Tuckwell, 2012). At +10 mV, the Cav1.2 antagonists: nifedipine, verapamil and calciseptine irreversibly blocked IBa with  IC50s of 2.2 µM (0.9 to 6; n=5), 49 nM (27 to 94; n=7) and 3.3 nM (1.7 to 6.7; n=6) respectively. At +10 mV, the Cav1.2 agonist BAYK 8644 enhanced IBa by 218 % (195 to 246) with an EC50 of 0.1 µM (0.03-0.4; n=8) whereas FPL 64176 potentiated IBa by 403 % (300 to 600) with an EC50 of 0.9 µM (0.11 to 12; n=7). These values were insignificantly different to those for  brain CaV1.2 except for verapamil, had an IC50 of 330 nM (140 to 800; n=4)  similar to that previously published of 339 nM for this brain channel isoform (Johnson et al., 1996). This study extends our knowledge about the  properties of CaV1.2 in adipocyte. One possible consequence of the extension between exons 9 and 10 of the WFA CaV1.2 a1 subunit is the 10 fold enhanced potency to verapamil.