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T1327

Sigma-Aldrich

Tissue Inhibitor of Metalloproteinase-3 human

recombinant, expressed in NSO cells, >95% (SDS-PAGE)

Synonym(s):

TIMP-3

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in NSO cells

Assay

>95% (SDS-PAGE)

form

lyophilized powder

mol wt

apparent mol wt ~30 kDa

technique(s)

inhibition assay: suitable

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... TIMP3(7078)

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General description

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.

Biochem/physiol Actions

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.
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.

Physical form

Lyophilized from a 0.2 μm filtered solution in 25 mM Tris and 0.15 M sodium chloride, pH 7.5.

Analysis Note

The biological activity is measured by its ability to inhibit human MMP-2 hydrolysis of a peptide substrate.

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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

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