The low-density lipoprotein receptor-related protein-1 (LRP1), identical to the Alpha2-macroglobulin receptor (A2MR), is a member of the LDL receptor superfamily. The ubiquitously expressed LRP1 in particular is a scavenger receptor that mediates clearance of over 50 ligands from the extracellular matrix and the bloodstream among others A2M, proteases, and distinct components involved in modulation of cancer cell dissemination. Moreover, LRP1 is implicated in coordinating cell-matrix interactions, cell migration, as well as tumour promotion. So far, LRP1 was associated with both anti-tumour and recently with pro-invasive functions, thus indicating a more complex functionality. Beyond that LRP1 is involved in regulation of signalling pathways and physiologic processes such as regulation of lipid metabolism and the proliferation of vascular smooth muscle cells. NCBI data bank research revealed the expression of a truncated splice variant of LRP1 mRNA (shLRP1). Using standard PCR and Western Blot both its mRNA transcript and protein expression was analysed in human tissues and cancer samples as well as cancer cell lines. In order to localise the shLRP1 protein in cells, shLRP1 protein was over-expressed in cancer cell lines using pcDNA3.1 vector and Lipofectamine and analysed using immune fluorescence microscopy. The gene LRP1 comprising 84.86 kb is localised on chromosome 12q13.3 and is organised in 89 exons coding for a mature mRNA transcript of 14886 nucleotides. Compared to LRP1, the shLRP1 comprises exon 1 – 6 of LRP1 followed by an alternative exon containing a polyadenylation signal. As a result, the respective transcript shLRP1 can escape nonsense-mediated decay. Hence, the shLRP1 mRNA code for a truncated protein of only 296 aa exhibiting a unique C-terminus in contrast to LRP1 comprising 4544 aa. The shLRP1 mRNA was detected to be exclusively present in several solid tumours. Beyond that it was also present in tumours of brain, breast, colon, lung, muscle, and prostate as well as in corresponding tumour cell lines, such as U87-MG, 1321N1 (astrocytoma), MDA-MB-231, HT-29 (colon), A549 (lung), and PC3 (prostate). In contrast, no expression was detected in tumour cells derived from blood cells as well as normal human tissue. Western blot analysis of protein extracts of several cancer cell lines among others 1321N1, PC3, HT-29, and A549 verified translation of shLRP1 mRNA into protein. Consequently, shLRP1, over-expressed in transfected cancer cell lines, was detected in the cytoplasm and the perinuclear region, but not – as the LRP1 – in the cell membrane. Summarising, these preliminary data offer the possibility to exploit the shLRP1 for tumour diagnosis, and tumour therapy on the one hand. On the other hand, the limited expression of shLRP1 in cancer cells raises the question regarding its involvement in physiological signalling pathways that have to be further investigated.