A substrate-optimized electrophoretic mobility shift assay for ADAM12.
Anal Biochem
; 452: 34-42, 2014 May 01.
Article
en En
| MEDLINE
| ID: mdl-24534253
ABSTRACT
ADAM12 belongs to the A disintegrin and metalloprotease (ADAM) family of secreted sheddases activating extracellular growth factors such as epidermal growth factor receptor (EGFR) ligands and tumor necrosis factor-alpha (TNF-α). ADAM proteases, most notably ADAM17 (TNF-α-converting enzyme), have long been investigated as pharmaceutical drug targets; however, due to lack of potency and in vivo side effects, none of the small-molecule inhibitors discovered so far has made it beyond clinical testing. Ongoing research on novel selective inhibitors of ADAMs requires reliable biochemical assays to validate molecular probes from large-scale screening efforts. Here we describe an electrophoretic mobility shift assay for ADAM12 based on the identification of an optimized peptide substrate that is characterized by excellent performance and reproducibility.
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Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Péptidos
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Ensayo de Cambio de Movilidad Electroforética
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Proteínas ADAM
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Proteínas de la Membrana
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Anal Biochem
Año:
2014
Tipo del documento:
Article