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Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. De plus, nous expédions AQPEP Kits (8) et AQPEP Anticorps (4) et beaucoup plus de produits pour cette protéine.
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Laeverin is expressed in all trophoblast cell types of normal and preeclamptic placentas. Expression pattern of laeverin in trophoblast cells is heterogeneous and not necessarily membrane-bound.
In preeclamptic placentas, laeverin is experssed in the cytoplasm and microvesicles, rather than the cell membrane. Laeverin appears to be involved in trophoblast cell migration and invasion through interaction with integrins and matrix metalloprotease 1.
Laeverin is a specific cell-surface marker for human extravillous trophoblast (EVT) and plays a regulatory role in EVT migration.
Replacement of glutamine-238 with alanine caused a significant change in substrate specificity rather than a decrease in enzymatic activity.
These results indicate that His(379) of laeverin plays essential roles in its distinctive enzymatic properties and contributes to maintaining the appropriate structure of the catalytic cavity of the enzyme.
Extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases(laeverin)
The 3 most significantly overexpressed genes in rheumatoid arthritis were laeverin, 11beta-hydroxysteroid dehydrogenase type 2 (a steroid pathway enzyme), and cysteine-rich, angiogenic inducer 61 (a known angiogenic factor).
is a novel bestatin-sensitive leucine aminopeptidase; plays important roles in human placentation by regulating biological activity of key peptides at the embryo-maternal interface
A novel membrane-bound cell surface peptidase, laeverin (FLJ90650), was found to be specifically expressed on extravillous trophoblasts that had almost ceased invasion into maternal decidual tissues.
Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
, CHL2 antigen