T1327
Tissue Inhibitor of Metalloproteinase-3
recombinant, expressed in NSO cells, >95% (SDS-PAGE)
Sinonimo/i:
TIMP-3
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10 μG
343,00 €
343,00 €
Prezzo di listino686,00 €Risparmia il 50%Per informazioni sulla disponibilità, contatta il Servizio Clienti.
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Cambia visualizzazione
10 μG
343,00 €
About This Item
343,00 €
Prezzo di listino686,00 €Risparmia il 50%Per informazioni sulla disponibilità, contatta il Servizio Clienti.
Prodotti consigliati
Origine biologica
human
Livello qualitativo
Ricombinante
expressed in NSO cells
Saggio
>95% (SDS-PAGE)
Stato
lyophilized powder
PM
apparent mol wt ~30 kDa
tecniche
inhibition assay: suitable
N° accesso UniProt
Temperatura di conservazione
−20°C
Informazioni sul gene
human ... TIMP3(7078)
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Descrizione generale
Tissue inhibitor of metalloproteinases 3 (TIMP3) is localized in the extracellular matrix (ECM) of epithelial cells associated with kidneys, eyes and lungs.[1] It is majorly secreted in retinal pigment epithelium (RPE).[2] TIMP3 gene is mapped to human chromosome 22q12.3[1] and is a CLOCK-dependent diurnal gene.[3] TIMP proteins display a three-lobed structure and have conserved cysteine residues.[2]
Azioni biochim/fisiol
The TIMPs are endogenous inhibitors of the matrix metalloproteinases (MMPs). TIMP-3 inhibits ADAM-17 (TACE) at nanomolar concentrations and also inhibits other metalloproteinases (sheddases) that mediate the shedding of soluble receptors and other proteins from the surface of cells.
Tissue inhibitor of metalloproteinases 3 (TIMP3) is a matrix metalloproteinase inhibitor.[3] TIMP proteins comprise the N-terminal region, which aids in the matrix metalloproteinase interaction. The C-terminal region is crucial for extracellular matrix (ECM) interaction.[2] Elevated expression of TIMP3 favors apoptosis in cancer types.[3] Its interaction with the vascular endothelial growth factor (VEGFR-2) leads to the regulation of angiogenesis.[1] TIMP3 also aids in protection against ultra-violet (UV)-induced cellular responses.[3] Missense mutations in the TIMP3 gene are implicated in Sorsby′s fundus dystrophy (SFD).[1] Mutations in the TIMP3 gene also leads to increased accumulation of the protein resulting in the thickening of the Bruch membrane. This, in turn, reduces membrane permeability towards nutrients and metabolites.[2]
Stato fisico
Lyophilized from a 0.2 μm filtered solution in 25 mM Tris and 0.15 M sodium chloride, pH 7.5.
Risultati analitici
The biological activity is measured by its ability to inhibit human MMP-2 hydrolysis of a peptide substrate.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 1
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
dust mask type N95 (US), Eyeshields, Gloves
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Daniel Ardeljan et al.
European journal of human genetics : EJHG, 21(10), 1152-1157 (2013-02-21)
Age-related macular degeneration (AMD) is a leading cause of irreversible central visual loss in the elderly. A recent genome-wide association studies (GWAS) reported that rs9621532 near the tissue inhibitor of metalloproteinase 3 (TIMP3)/synapsin III (SYN3) region of 22q12.3 is associated
Sunyoung Park et al.
International journal of molecular sciences, 20(4) (2019-02-20)
The human skin is the outermost physical barrier and has its own circadian machinery that works either cooperatively with the central clock, or autonomously. Circadian rhythms have been observed in many functions related to epidermal homeostasis including hydration and inflammation
Ruth Appeltant et al.
Animal science journal = Nihon chikusan Gakkaiho, 88(9), 1279-1290 (2017-01-27)
In vitro maturation (IVM) in serum causes hampered expansion of porcine cumulus-oocyte complexes (COCs) due to excessive alpha
K J Leco et al.
The Journal of biological chemistry, 269(12), 9352-9360 (1994-03-25)
We have isolated cDNA clones corresponding to a novel mouse metalloproteinase inhibitor. Five overlapping cDNA clones contain most of the information for a prominent 4.5-kilobase transcript that was detected in RNA from mouse fibroblasts and adult tissues. Sequence analysis revealed
A Amour et al.
FEBS letters, 435(1), 39-44 (1998-10-02)
TNF-alpha converting enzyme (TACE; ADAM-17) is a membrane-bound disintegrin metalloproteinase that processes the membrane-associated cytokine proTNF-alpha to a soluble form. Because of its putative involvement in inflammatory diseases, TACE represents a significant target for the design of specific synthetic inhibitors
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