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dc.contributor.authorSafdari, Y
dc.contributor.authorFarajnia, S
dc.contributor.authorAsgharzadeh, M
dc.contributor.authorKhosroshahi, SA
dc.contributor.authorVeisi, K
dc.contributor.authorAhmadzadeh, V
dc.contributor.authorKhalili, M
dc.date.accessioned2018-08-26T06:06:31Z
dc.date.available2018-08-26T06:06:31Z
dc.date.issued2013
dc.identifier.urihttp://dspace.tbzmed.ac.ir:8080/xmlui/handle/123456789/42014
dc.description.abstractThe current study was aimed at introducing an efficient enzyme-conjugated molecule for use in the detection of humanized single chain antibodies. Because they are composite in their variable domain sequences and also devoid of constant domains, humanized single chain antibodies require a suitable secondary enzyme-conjugated antibody (more precisely enzyme-conjugated protein molecule) to be efficiently recognized and detected in ELISA, dot blot, and other detection tests, guaranteeing a more precise evaluation of their quantity, affinity, and other features. In the current study we examined the ability of three HRP-conjugated protein molecules including protein L, anti-human IgG antibody, and anti-mouse IgG antibody in the detection of three humanized single chain antibodies (anti-CD20, anti-EGFRvIII, and anti-EGFR) in ELISA and dot blot tests. The results signify the HRP-conjugated protein L as the most efficient molecule for detecting humanized single chain antibody.
dc.language.isoEnglish
dc.relation.ispartofMonoclonal antibodies in immunodiagnosis and immunotherapy
dc.subjectAnimals
dc.subjectBacterial Proteins
dc.subjectEnzyme-Linked Immunosorbent Assay
dc.subjectHorseradish Peroxidase
dc.subjectHumans
dc.subjectImmunoblotting
dc.subjectMice
dc.subjectSingle-Chain Antibodies
dc.titleProtein L: a robust enzyme-conjugated molecule for detection of humanized single chain antibodies.
dc.typearticle
dc.citation.volume32
dc.citation.issue6
dc.citation.spage409
dc.citation.epage12
dc.citation.indexPubmed
dc.identifier.DOIhttps://doi.org/10.1089/mab.2013.0049


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