{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mesa RA"],"funding":["NCATS NIH HHS","NIAMS NIH HHS"],"pagination":["1211"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7194342"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8"],"pubmed_abstract":["Nicastrin (NCSTN) is a transmembrane glycoprotein that is part of the gamma-secretase complex. Gamma-secretase is a protease complex that cleaves type-I single-pass transmembrane proteins. There are many potential substrates for this complex, including NOTCH receptors and amyloid precursor proteins (APP). There are a number of commercial antibodies to nicastrin, but they do not agree on expected peptide size. We confirmed the specificity of a C-terminal binding rabbit anti-human antibody from Sigma-Aldrich (#N1660) using wildtype HEK293 cells and HEK293 cells deleted for nicastrin. The wildtype cells showed a prominent band at approximately 110 kDa. We confirmed this larger than expected sized was due to glycosylation by treating the lysate with peptide-N-glycosidase F (PNGase F), which re"],"journal":["F1000Research"],"pubmed_title":["Validation of a commercial antibody to detect endogenous human nicastrin by immunoblot."],"pmcid":["PMC7194342"],"funding_grant_id":["P30 AR073752","UL1 TR000448"],"pubmed_authors":["Mesa RA","Roberson EDO"],"additional_accession":[]},"is_claimable":false,"name":"Validation of a commercial antibody to detect endogenous human nicastrin by immunoblot.","description":"Nicastrin (NCSTN) is a transmembrane glycoprotein that is part of the gamma-secretase complex. Gamma-secretase is a protease complex that cleaves type-I single-pass transmembrane proteins. There are many potential substrates for this complex, including NOTCH receptors and amyloid precursor proteins (APP). There are a number of commercial antibodies to nicastrin, but they do not agree on expected peptide size. We confirmed the specificity of a C-terminal binding rabbit anti-human antibody from Sigma-Aldrich (#N1660) using wildtype HEK293 cells and HEK293 cells deleted for nicastrin. The wildtype cells showed a prominent band at approximately 110 kDa. We confirmed this larger than expected sized was due to glycosylation by treating the lysate with peptide-N-glycosidase F (PNGase F), which re","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2025-04-19T17:43:50.159Z","creation":"2020-05-22T20:12:37Z"},"accession":"S-EPMC7194342","cross_references":{"pubmed":["32399180"],"doi":["10.12688/f1000research.19803.2"]}}