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The extracellular matrix (ECM) plays an essential role in tumor progression and invasion through its continuous remodeling. The growth of most carcinomas is associated with an excessive collagen deposition that provides the proper environment for tumor development and chemoresistance. The α1 chain of a minor human collagen, type XI, is overexpressed in some tumor stroma, but not found in normal stroma. To test the clinical utility of this collagen as a cancer biomarker, specific receptors are needed. Available antibodies do not show enough selectivity or are directed toward the propeptide region that is cleaved when the protein is released to the ECM. Here we show the selection of an aptamer for the specific C-telopeptide region using a 16-mer peptide as the target for the SELEX. The aptamer selected with a K d of ∼25 nM was able to capture the collagen XI from cell lysates. It was also used for target detection in a mixed antibody-aptamer sandwich assay showing it can be useful for diagnostic purposes in biological fluids. [Display omitted] • Extracellular matrix components are an understudied source of cancer biomarkers. • Detection of collagen XI, overexpressed in some cancers, needs suitable probes. • A 16mer peptide was the target for the first aptamer for α chain of human collagen XI. • Mass spectrometry verifies collagen XI as the target of D1 aptamer from cell lysates. • Antibody-aptamer sandwich assay detects colXIα1 in cell lysates. [ABSTRACT FROM AUTHOR]