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MMP-9 (catalytic domain) (human), (recombinant, E. coli)

 
BML-SE360-0010 10 µg 384.00 USD
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  • Naturally-occurring active form of MMP-9
  • High purity
  • High activity

Product Specification

Alternative Name:Matrix metalloproteinase 9, Gelatinase B, 92 kDa Type IV collagenase
 
MW:39 kDa
 
Source:Produced in E. coli. Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin, casein, or peptide substrates, is unaffected.
 
UniProt ID:P14780
 
Formulation:Liquid. In 50mM TRIS, pH 7.5, containing 1mM calcium chloride, 300mM sodium chloride, 5μM zinc chloride, 0.1% Brij-35 and 15% glycerol.
 
Purity:≥95% (SDS-PAGE)
 
Purity Detail:Purified by multi-step chromatography.
 
Activity:Preincubation of MMP-9 catalytic domain at 1.3nM with the broad-spectrum inhibitor GM6001 (Prod. No. BML-EI300) at 30nM for 1 hour inhibits enzymatic activity by 97%.
 
Specific Activity:≥20 U/µg. One U=100pmol/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:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -80°C.
 
Scientific Background:Matrix metallopeptidase 9 (MMP-9) belongs to a class of enzymes that belong to the zinc-metalloproteinase family involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory. Its also associated with numerous pathological processes, including cancer, immunologic and cardiovascular diseases.
 
BML-SE360 SDS-PAGE
SDS-PAGE Analysis: Lane 1: MW Marker, Lane 2: 1μg MMP-9 (catalytic domain) (human), (recombinant, E. coli).
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BML-SE360 SDS-PAGE

Product Literature References

Active Matrix Metalloprotease-9 Is Associated with the Collagen Capsule Surrounding the Madurella mycetomatis Grain in Mycetoma: K. Geneugelijk, et al.; PLoS Negl. Trop. Dis. 8, e2754 (2014), Application(s): Gelatin Zymography, Abstract; Full Text
Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines: A. Jabaiah, et al.; Chem. Biol. 18, 392 (2011), Abstract; Full Text
IL-1β Is Overexpressed and Aberrantly Regulated in Corticosteroid Nonresponders with Autoimmune Inner Ear Disease: S. Pathak, et al.; J. Immunol. 186, 1870 (2011), Application(s): Cell Culture, Abstract; Full Text

General Literature References

New strategy for antedrug application: development of metalloproteinase inhibitors as antipsoriatic drugs: M. Sawa, et al.; J. Med. Chem. 45, 930 (2002), Abstract;
Matrix metalloproteinases: they’re not just for matrix anymore!: L.J. McCawley & L.M. Matrisian; Curr. Opin. Cell Biol. 13, 534 (2001), Abstract;
Structural properties of matrix metalloproteinases: W. Bode, et al.; Cell. Mol. Life Sci. 55, 639 (1999), Abstract;
Relating matrix metalloproteinase structure to function: why the "hemopexin" domain?: G. Murphy & V. Knauper; Matrix Biol. 15, 511 (1997), Abstract;
Mechanism of activation of human neutrophil gelatinase B. Discriminating between the role of Ca2+ in activation and catalysis: C.H. Bu & T. Pourmotabbed; J. Biol. Chem. 270, 18563 (1995), Abstract;
Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B: J.P. O'Connell, et al.; J. Biol. Chem. 269, 14967 (1994), Abstract;
Matrix metalloproteinases: a review: H. Birkedal-Hansen, et al.; Crit. Rev. Oral Biol. Med. 4, 197 (1993), Abstract;
SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages: S.M. Wilhelm, et al.; J. Biol. Chem. 264, 17213 (1989), Abstract;

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