{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["61(3)"],"submitter":["Nollau P"],"pubmed_abstract":["Specialized protein domains bind to posttranslational modifications (PTMs) of proteins, such as phosphorylation or glycosylation. When such PTM-binding protein domains are used as analytical tools, the functional states of cells and tissues can be determined with high precision. Here, we describe the use of recombinant CLEC10A (CD301), a human glycoreceptor of the C-type lectin family, for the detection of ligands in sections from formalin-fixed, paraffin-embedded normal and cancerous mammary tissues. A construct, in which part of the carbohydrate recognition domain (CRD) was deleted, was used as a negative control. In comparison to normal mammary glands, a pronounced staining of tumor tissues was observed. Because the construct with the truncated CRD did not show any tissue staining, the "],"journal":["The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society"],"pagination":["199-205"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3636699"],"repository":["biostudies-literature"],"pubmed_title":["Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues."],"pmcid":["PMC3636699"],"pubmed_authors":["Wolters-Eisfeld G","Bockhorn M","Mortezai N","Klampe B","Kurze AK","Niendorf A","Wagener C","Debus A","Nollau P"],"additional_accession":[]},"is_claimable":false,"name":"Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.","description":"Specialized protein domains bind to posttranslational modifications (PTMs) of proteins, such as phosphorylation or glycosylation. When such PTM-binding protein domains are used as analytical tools, the functional states of cells and tissues can be determined with high precision. Here, we describe the use of recombinant CLEC10A (CD301), a human glycoreceptor of the C-type lectin family, for the detection of ligands in sections from formalin-fixed, paraffin-embedded normal and cancerous mammary tissues. A construct, in which part of the carbohydrate recognition domain (CRD) was deleted, was used as a negative control. In comparison to normal mammary glands, a pronounced staining of tumor tissues was observed. Because the construct with the truncated CRD did not show any tissue staining, the ","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Mar","modification":"2025-04-04T10:35:28.416Z","creation":"2019-03-27T01:07:56Z"},"accession":"S-EPMC3636699","cross_references":{"pubmed":["23275449"],"doi":["10.1369/0022155412474823"]}}