ADAM-15 (MDC-15, metargidin) is a membrane-anchored disintegrin and metalloprotease that is present on the cell surface. ADAM-15 may play a role in cell-cell interactions through its association with integrins. Studies have reported that ADAM15 is involved in the migration of mesangial cells. Rabbit anti-ADAM-15, cytoplasmic domain antibody localizes human ADAM15. By immunoblotting against the reduced protein, the antibody recognizes bands of 110kDa (zymogen) and 90kDa (furin-processed form) of ADAM15. A series of cleaved products at 55kDa and 40kDa can also be seen in reduced immunoblots of cell lysates.
Immunogen
synthetic peptide corresponding to the cytoplasmic domain of human ADAM-15.
Application
Rabbit anti-ADAM-15, cytoplasmic domain antibody can be used for western blot applications at 1:1,000.
Physical form
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
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The Journal of biological chemistry, 273(13), 7345-7350 (1998-04-29)
MDC-15 (ADAM-15, metargidin), a membrane-anchored metalloprotease/disintegrin/cysteine-rich protein, is expressed on the surface of a wide range of cells and has an RGD tripeptide in its disintegrin-like domain. MDC-15 is potentially involved in cell-cell interactions through its interaction with integrins. We
The Journal of biological chemistry, 277(37), 33683-33689 (2002-07-02)
Mesangial cells (MC) occupy the core of the renal glomerulus and are surrounded by a mesangial matrix. In certain diseases, MC migrate through this matrix into the pericapillary space. The mechanisms involved, however, are poorly understood. Members of the ADAM
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