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ADAMTS10 belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. Zusätzlich bieten wir Ihnen ADAMTS10 Antikörper (49) und ADAMTS10 Proteine (4) und viele weitere Produktgruppen zu diesem Protein an.
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ADAMTS10 is identified as a potential functional integrator of the Ikaros (zeige IKZF1 ELISA Kits)-CtBP (zeige CTBP2 ELISA Kits) chromatin remodeling network.
these studies support the notion that sperm-oocyte interactions involve considerable functional redundancy and identify ADAMTS10 as a novel candidate in the mediation of these fundamentally important events.
TGF-beta (zeige TGFB1 ELISA Kits) stimulation of renal cells results in a significant up-regulation of Adams 10, 17, 12, and 19
ADAMTS10 is a functional metalloprotease (zeige ADAMTS7 ELISA Kits) as demonstrated by cleavage of alpha2-macroglobulin (zeige A2M ELISA Kits)
Using siRNA, over-expression and mutagenesis, it was found ADAMTS6 (zeige ADAMTS6 ELISA Kits) inhibits and ADAMTS10 is required for focal adhesions, epithelial cell-cell junction formation, and microfibril deposition.
These findings support the Gly661Arg mutation of ADAMTS10 as the likely cause of POAG in beagles.
ADAMTS10 participates in microfibril biogenesis rather than in fibrillin-1 (zeige FBN1 ELISA Kits) turnover
ADAMTS10 is a functional metalloprotease as demonstrated by cleavage of alpha2-macroglobulin (zeige A2M ELISA Kits)
ADAMTS10 plays a major role in growth and in skin, lens, and heart development in humans.
infer that folding of the complex C-terminal ancillary domain is the rate-limiting step in biosynthesis of ADAMTS10, and that it (but not catalytic domain) is sensitive to subtle changes in efficiency of signal peptide cleavage.
Mutations in ADAMTS10 gene is not responsible for microspherophakia.
Homozygous mutation in ADAMTS10 causes lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature.
This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome.
A disintegrin and metalloproteinase with thrombospondin motifs 10
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 10
, zinc metalloendopeptidase
, ADAM-TS 10
, ADAM metallopeptidase with thrombospondin type 1 motif 10
, a disintegrin-like and metalloprotease with thrombospondin type 1 motif, 10