<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>61(3)</volume><submitter>Nollau P</submitter><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 </pubmed_abstract><journal>The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society</journal><pagination>199-205</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3636699</full_dataset_link><repository>biostudies-literature</repository><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.</pubmed_title><pmcid>PMC3636699</pmcid><pubmed_authors>Wolters-Eisfeld G</pubmed_authors><pubmed_authors>Bockhorn M</pubmed_authors><pubmed_authors>Mortezai N</pubmed_authors><pubmed_authors>Klampe B</pubmed_authors><pubmed_authors>Kurze AK</pubmed_authors><pubmed_authors>Niendorf A</pubmed_authors><pubmed_authors>Wagener C</pubmed_authors><pubmed_authors>Debus A</pubmed_authors><pubmed_authors>Nollau P</pubmed_authors></additional><is_claimable>false</is_claimable><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.</name><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 </description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Mar</publication><modification>2025-04-04T10:35:28.416Z</modification><creation>2019-03-27T01:07:56Z</creation></dates><accession>S-EPMC3636699</accession><cross_references><pubmed>23275449</pubmed><doi>10.1369/0022155412474823</doi></cross_references></HashMap>