Human MMP-9, His Tag (MM9-H5221) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 469 (Accession # AAH06093).
Predicted N-terminus: Ala 20
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 50.8 kDa. The protein migrates as 55-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
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, Sigma, Catalog # A-9563) 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.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
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.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human MMP-9, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
Matrix metallopeptidase 9 (MMP-9) is 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.
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