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Recombinant human MMP9 Protein, His tag, 50µg  

Recombinant human MMP9 Protein, His tag, 50µg

Recombinant human MMP9 Protein, Ala20-Pro469, expressed in HEK293 cells, His tag

recombinant, human, protein, MMP9, CLG4B, GELB, MANDP2, MMP-9, Matrix metallopeptidase 9, matrix metalloproteinase

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420,00 €

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Thrombospondins, intervertebral disc proteins, regulate the effective levels of matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling.[1]
Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. . Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.[2]

Recombinant human MMP9 Protein (rhMMP9), Ala20-Pro469 (Accession# AAH06093) was expressed in HEK293 cells.

Molecular Characterization
rhMMP9, a 450 amino acids protein with polyhistidine tag at C-terminus, and has a calculated MW of 50.8 kDa. The predicted N-terminal is Ala20. DTT-reduced protein migrates as 55-65 kDa protein due to different glycosylation.

Less than 1.0 EU per μg of the or rhMMP9 by the LAL method.

>95% purity as determined by SDS-PAGE of reduced rhMMP9.

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, pH7.5. Normally trehalose is added as protectant before lyophilization.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Enzymatic Activity
Pre-activation is required for enzymatic assays. Please dilute Human MMP-9 to 100 µg/mL in TCNB buffer (50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 (w/v), pH 7.5), and then add p-aminophenylmercuric acetate (APMA) to a final concentration of 1 mM. Please keep the enzyme with APMA for 8-24 hour at 37°C. Please note that the optimal treatment time may need to be determined empirically.
100mM APMA stock solution should be prepared in DMSO. Please avoid adding high concentration APMA solution (>20mM) directly into the reaction as it tends to precipitate. A pre-dilution step is highly recommended.


(1) Hirose Y, et al., 2008, Am. J. Hum. Genet. 82 (5): 1122–9.
(2) Mira, E. et al., 2004, J. Cell. Sci. 117:1847-1857.