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SAE0078 Sigma-Aldrich

MMP-9 pre-activated human

recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells

Synonym: GELB, GELBCLG4B, Gelatinase B, Gelatinase, MANDP2, MMP-9, Matrix Metalloproteinase-10, Type IV collagenase

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Properties

Related Categories Application Index, Biochemicals and Reagents, Cell Signaling Enzymes, Enzymes, Inhibitors, and Substrates, MMP Enzymes,
Quality Level   200
biological source   human
recombinant   expressed in HEK 293 cells
assay   ≥95% (SDS-PAGE)
form   liquid
mol wt   calculated mol wt 66 kDa
  observed mol wt 82 kDa by SDS-PAGE (The protein migrates as a 82 kDa protein on SDS-PAGE due to glycosylation)
concentration   30-120 μg/mL (50 μg protein, determined by Bradford. The protein concentration is 30-120 μg/ml. for the lot-specific concentration, see Certificate of Analysis.)
application(s)   cell analysis: suitable
UniProt accession no.   P14780
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... MMP(4318)

Description

General description

Recombinant human pre-activated Matrix Metalloproteinase-9 (MMP-9) is expressed in human HEK 293 cells as a glycoprotein. The DTT-reduced protein migrates as a ~67 kDa polypeptide on SDS-PAGE. 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.

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.
As with most MMPs, MMP-9 is secreted as an inactive pro-protein which is activated when cleaved by extracellular proteinases. MMP-9 can be cleaved (and thus activated) in vitro using 4-Aminophenylmercuric acetate (APMA), Cat. No. A9563. 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.
As with most MMPs, MMP-9 is secreted as an inactive pro-protein which is activated when cleaved by extracellular proteinases. This product was cleaved and activated in vitro using 4-Aminophenylmercuric acetate (APMA), Cat. No. A9563.

Other Notes

This product was pre-activated in vitro using 4-Aminophenylmercuric acetate (APMA). Thus, it is active and ready for use. In order to save our customers from handling hazardous materials, and for environmental saving, the highly toxic and fatal APMA was removed from the final preparation.

Physical form

Liquid solution, 0.22 mm filtered, containing 25 mM Tris, 10 mM CaCl2, 0.05% Brij-35

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 3
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable
Protocols & Articles
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