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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

Catalog Number PKG Qty. Price Quantity
45-SAE0077-50UG 50 µg
$550.00
1/EA
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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 30-120 μg/mL (50 μg protein, determined by Bradford. For the lot-specific concentration, see Certificate of Analysis.)
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: 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 12352200

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