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MMP-19 (catalytic domain) (human), (recombinant)

BML-SE561-0010 10 µg 416.00 USD
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Product Details

Alternative Name:Matrix metalloproteinase 19, RASI
Sequence:Recombinant MMP-19 corresponding to aa Leu99-Ser259 (NM_002429), which comprises the catalytic domain of human MMP-19, with a C-terminal purification tag.
MW:19.2 kDa
Source:Produced in E.coli. Active recombinant MMP-19.
UniProt ID:Q99542
Formulation:Liquid. In 25mM NaBorate, pH 9.3, containing 5mM CaCl2, 20μM ZnCl2, 0.05% Brij-35 and 20% glycerol.
Purity:≥95% (SDS-PAGE)
Purity Detail:Purified by multi-step chromatography.
Activity:Preincubation of MMP-19 catalytic domain at 1.9µM with the broad-spectrum inhibitor GM6001 (Prod No. BML-EI300) at 100nM for 30 minutes only weakly inhibits enzymatic activity (27%).
Specific Activity:≥ 0.40U/µg. One U=100 pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100µM; Prod. No. BML-P125) as substrate.
Application Notes:Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Use/Stability:When stored under the recommended conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution followed by refreezing could lead to loss of activity.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
Scientific Background:MMP-19 is expressed widely, and degrades aggrecan, fibronectin, type I gelatin, and basement membrane components such as laminin, nidogen, and type IV collagen. It is involved in angiogenesis, cancer, rheumatoid arthritis, multiple sclerosis, and psoriasis.
Regulatory Status:RUO - Research Use Only
MMP-19 (catalytic domain) (human), (recombinant) SDS-PAGE
SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 0.5 µg of Purified MMP-19 (catalytic domain) (human) (rec.) Prod. No. BML-SE561.
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MMP-19 (catalytic domain) (human), (recombinant) SDS-PAGE

General Literature References

Matrix metalloproteinase-19 is highly expressed in astroglial tumors and promotes invasion of glioma cells: I. Lettau, et al.; J. Neuropathol. Exp. Neurol. 69, 215 (2010), Abstract;
MMP19 is upregulated during melanoma progression and increases invasion of melanoma cells: M. Muller, et al.; Mod. Pathol. 23, 511 (2010), Abstract;
VEGF and angiogenesis in acute and chronic MOG((35-55)) peptide induced EAE: W.A. Roscoe, et al.; J. Neuroimmunol. 209, 6 (2009), Abstract;
Matrix metalloproteinase-19 is highly expressed in active multiple sclerosis lesions: J. van Horssen, et al.; Neuropathol. Appl. Neurobiol. 32, 585 (2006), Abstract;
Matrix metalloproteinase-19 is expressed by keratinocytes in psoriasis: S. Suomela, et al.; Acta. Derm. Venereol. 83, 108 (2003), Abstract;
Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme: J.O. Stracke, et al.; J. Biol. Chem. 275, 14809 (2000), Abstract;
Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP): J.O. Stracke, et al.; FEBS Lett. 478, 52 (2000), Abstract;
Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution: A.M. Pendas, et al.; J. Biol. Chem. 272, 4281 (1997), Abstract;
The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient: C. Kolb, et al.; Immunol. Lett. 57, 83 (1997), Abstract;
Identification of MMP-18, a putative novel human matrix metalloproteinase: J. Cossins, et al.; Biochem. Biophys. Res. Commun. 228, 494 (1996), Abstract;

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