Összes fotó(1)
Fontos dokumentumok
T1327
Tissue Inhibitor of Metalloproteinase-3 human
recombinant, expressed in NSO cells, >95% (SDS-PAGE)
Szinonimák:
TIMP-3
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
biológiai forrás
human
Minőségi szint
rekombináns
expressed in NSO cells
Teszt
>95% (SDS-PAGE)
Forma
lyophilized powder
molekulatömeg
apparent mol wt ~30 kDa
technika/technikák
inhibition assay: suitable
UniProt elérési szám
tárolási hőmérséklet
−20°C
Géninformáció
human ... TIMP3(7078)
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Általános leírás
Tissue inhibitor of metalloproteinases 3 (TIMP3) is localized in the extracellular matrix (ECM) of epithelial cells associated with kidneys, eyes and lungs. It is majorly secreted in retinal pigment epithelium (RPE). TIMP3 gene is mapped to human chromosome 22q12.3 and is a CLOCK-dependent diurnal gene. TIMP proteins display a three-lobed structure and have conserved cysteine residues.
Biokémiai/fiziológiai hatások
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. 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. Elevated expression of TIMP3 favors apoptosis in cancer types. Its interaction with the vascular endothelial growth factor (VEGFR-2) leads to the regulation of angiogenesis. TIMP3 also aids in protection against ultra-violet (UV)-induced cellular responses. Missense mutations in the TIMP3 gene are implicated in Sorsby′s fundus dystrophy (SFD). 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.
Fizikai forma
Lyophilized from a 0.2 μm filtered solution in 25 mM Tris and 0.15 M sodium chloride, pH 7.5.
Analízis megjegyzés
The biological activity is measured by its ability to inhibit human MMP-2 hydrolysis of a peptide substrate.
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
dust mask type N95 (US), Eyeshields, Gloves
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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)
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In vitro maturation (IVM) in serum causes hampered expansion of porcine cumulus-oocyte complexes (COCs) due to excessive alpha
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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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
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