This study demonstrates that the putative ER-located Hsp90, XVGrp94, is upregulated under conditions of stress, and is the first report of such upregulation in response to desiccation stress. XVGrp94 was identified by differential screening of a cDNA library from a dehydrated resurrection plant Xerophyta viscosa Baker. Sequence analysis revealed that the cDNA potentially encoded a protein of 812 amino acids with a calculated molecular weight of 92.83kDa. Amino acid sequence comparisons revealed significant homology to several Grp94s from plants with the highest similarity to Grp94 from Oryza sativa (82.74%), Catharanthus roseus (81.97%), Hordeum vulgare (80.10%) and Arabidopsis thaliana (77.45%). The sequence contains the Hsp90 protein family signature, NKDIFL, a putative eukaryotic secretory signal, and the endoplasmic reticulum targeting and retention signal, KDEL. Residues that interact with ATP within the N-terminal domain of Hsp90s are conserved in the N-domain of the putative XVGrp94, indicating that it is potentially capable of ATP binding and hydrolysis. Southern blot analysis confirmed the presence of the XVGrp94 gene within the X. viscosa genome and the results suggest the possibility of homologues. Western blot analysis showed that the XVGrp94 expression increased significantly in response to heat and dehydration, and slightly in response to high salinity. No response was seen in response to high light, cold treatment or exogenous ABA (abscisic acid) application.