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ADAMTS5 encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Zusätzlich bieten wir Ihnen ADAMTS5 Antikörper (122) und ADAMTS5 Kits (39) und viele weitere Produktgruppen zu diesem Protein an.
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Adamts5(-/-) mice were protected from hepatic mitochondrial dysfunction, as indicated by increased mitochondrial respiratory chain complex activity, higher ATP levels and higher expression of antioxidant enzymes. Absence of ADAMTS5 preserves liver integrity in a diet-induced obesity model.
research emphasises the importance of ADAMTS5 expression in the control of influenza virus infection and highlights the potential for development of ADAMTS5-based therapeutic strategies to reduce morbidity and mortality
TS5 protein functions to suppress glucose uptake in adipose-derived stromal cells and thereby inhibits the synthesis, and promotes the intracellular degradation of Acan (zeige ACAN Proteine) and Vcan (zeige Vcan Proteine) by an ADAMTS (zeige ADAMTS1 Proteine) other than TS5.
Data suggest that ADAMTS-5 oligomerization is required for full aggrecanase (zeige ADAMTS4 Proteine) activity in vitro and in situ (as seen in knee joint of mouse model of inflammatory arthritis); thus, blocking oligomerization inhibits ADAMTS-5 activity.
aggrecan (zeige ACAN Proteine) and brevican (zeige BCAN Proteine) proteolysis is compensated in Adamts4 (zeige ADAMTS4 Proteine)-/- or Adamts5-/- mice by ADAMTS (zeige ADAMTS1 Proteine) proteoglycanase (zeige MMP3 Proteine) family members but a threshold of versican (zeige Vcan Proteine) proteolysis is sensitive to the loss of a single ADAMTS (zeige ADAMTS1 Proteine) proteoglycanase (zeige MMP3 Proteine) during spinal cord injury
The present study reveals ADAMT-5 expression by mast cells(MCs (zeige SMCP Proteine)) and that MC activation regulates the expression of the protease, thus implicating the ADAMT-5 of protease in MC function.
Western blot analyses indicated that aggrecanase (zeige ADAMTS4 Proteine)-generated proteoglycan (zeige Vcan Proteine) fragments are produced after SCI.
RelA/p65 (zeige NFkBP65 Proteine) is a potent transcriptional activator of ADAMTS5 in chondrocytes during osteoarthritis development.
Repair of biomechanically compromised tendons exhibiting midsubstance chondroid accumulation requires ADAMTS5.
this study identified, for the first time, several genes that have an ADAMTS-5-independent role in osteoarthritis(OA), identifying them as possible OA initiation candidates.
The IL1B (zeige IL1B Proteine)/AP-1 (zeige FOSB Proteine)/miR (zeige MLXIP Proteine)-30a/ADAMTS-5 axis regulates cartilage matrix degradation in osteoarthritis.
The findings suggest that miR (zeige MLXIP Proteine)-140 suppresses colorectal cancer progression and metastasis, possibly through downregulating ADAMTS5 and IGFBP5 (zeige IGFBP5 Proteine).
Results provide direct evidence indicating that Fibulin-2 (zeige FBLN2 Proteine) is a novel substrate of ADAMTS-5 and that this proteolysis could alter the cellular microenvironment affecting the balance between protumor and antitumor effects associated to both Fibulin-2 (zeige FBLN2 Proteine) and the ADAMTSs metalloproteases.
Endoplasmic reticulum stress participates in the progress of senescence and apoptosis of osteoarthritic chondrocytes, which manifested in increased expression of ADAMTS5, MMP13 (zeige MMP13 Proteine), and decreased COL2A1 (zeige COL2A1 Proteine) expression.
Single Nucleotide Variants of Candidate Genes in Aggrecan (zeige ACAN Proteine) Metabolic Pathway Are Associated with Lumbar Disc Degeneration and Modic Changes
RREB1 cooperates with noncoding RNA linc-ADAMTS5 to inhibit ADAMTS5 expression, thereby affecting degeneration of the extracellular matrix (ECM (zeige MMRN1 Proteine)) of the intervertebral disc.
Matrilin 2 (zeige MATN2 Proteine) accumulation associated with relative ADAMTS5 deficiency may contribute to the mechanism underlying calcific aortic valve disease progression.
In osteoarthritis (OA) chondrocytes, hydrostatic pressure (HP) restores the expression levels of some miRNAs, downregulates MMP-13 (zeige MMP13 Proteine), ADAMTS-5, and HDAC-4 (zeige HDAC4 Proteine), and modulates the Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) pathway activation.
we investigated whether important polymorphisms in the ADAMTS4 (zeige ADAMTS4 Proteine) and ADAMTS5 genes affect osteoarthritis (OA) susceptibility. ADAMTS4 (zeige ADAMTS4 Proteine) and ADAMTS5 genotypes were determined using the ABI Prism StepOnePlus Real-Time system. Our findings suggest that the ADAMTS4 (zeige ADAMTS4 Proteine) (rs4233367 and rs11807350) and ADAMTS5 (rs226794 and rs2830585) variants examined may not contribute to susceptibility to knee OA in the Turkish population.
Increased ADAMTS5 levels were observed in placental insufficiency cases.
The delayed activation of proMMPs and the relatively low cleavage efficiency of MMPs compared to ADAMTS5 (aggrecanase (zeige ADAMTS4 Proteine)) explains the minor contribution of the MMP enzymes to aggrecan (zeige ACAN Proteine) catabolism in vivo.
ADAMTS4 (zeige ADAMTS4 Proteine) and ADAMTS5 are inhibited by alpha2-macroglobulin (zeige A2M Proteine)
identified multiple conserved amino acids within regions N- and C-terminal to the site of scission that may influence enzyme-substrate recognition, and may interact with exosites on ADAMTS-4 (zeige ADAMTS4 Proteine) and ADAMTS-5
Co-culture of mechanically injured cartilage with joint capsule tissue alters chondrocyte expression patterns and increases ADAMTS5 production.
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage.
ADAM metallopeptidase with thrombospondin type 1 motif, 5
, a disintegrin and metalloproteinase with thrombospondin motifs 5-like
, A disintegrin and metalloproteinase with thrombospondin motifs 5
, ADAM-TS 5
, a disintegrin and metalloproteinase with thrombospondin motifs 11
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2)
, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5
, a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase-2)