MMP-9 human
SIGMA/SAE0077 - recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells
Synonym: GELBCLG4B; Gelatinase; Gelatinase B; MANDP2; MMP-9; Matrix Metalloproteinase-9; Type IV collagenase
Product Type: Chemical
MMP-9 human recombinant (Cat. No. SAE0077) was incubated with APMA in 37 °C. Samples of the designated time points were assessed on SDS-PAGE, followed by InstantBlue™ staining (Cat. No. ISB1L). Maximal activation was observed after 24 hours.
The activity of MMP-9 human recombinant (Cat. No. SAE0077) was measured using the MMP-9 fluorogenic substrate, MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2 (Cat. No. SCP0193), in the presence (green) or absence (red) of APMA.
| application(s) | cell analysis |
| assay | 95% (SDS-PAGE) |
| biological source | human |
| concentration | 50-200 μg/mL |
| form | liquid |
| mol wt | calculated mol wt 76 kDa |
| observed mol wt 92 kDa (The protein migrates as a 92 kDa protein on SDS-PAGE due to glycosylation) | |
| Quality Level | 200  |
| recombinant | expressed in HEK 293 cells |
| shipped in | dry ice |
| storage temp. | −20°C |
| UniProt accession no. | P14780  |
| Biochem/physiol Actions: | MMP-9 is a member of the matrix metalloproteinase (MMP) family of proteins. Proteins of the 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. Studies in rhesus monkeys suggest that MMP9 is involved in IL-8 (interleukin-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 MMP-2 and -9, which are key effectors of extracellular matrix (ECM) remodeling. MMP-9 degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 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. MMP-9 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 pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain. |
| General description: | 50 μg protein, determined by Bradford. For the lot-specific concentration, see Certificate of Analysis. |
| General description: | Recombinant human Matrix Metalloproteinase-9 (MMP-9) is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 76 kDa (amino acids 20-707). The DTT-reduced protein migrates as a ~92 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher specific activity of the protein. The protein is produced with no artificial tags. |
| Other Notes: | This product can be activated in vitro by adding 4-Aminophenylmercuric acetate (APMA), Cat. No. A9563, to a final concentration of 1 mM. |
| Physical form: | Liquid solution, 0.22 mm filtered, containing 25 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% Brij-35 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | 95% (SDS-PAGE) |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 3.4.24.35 ( BRENDA | IUBMB ) |
| UNSPSC | 12352202 |