SAE0078
MMP-9 pre-activated human
recombinant, ≥1,300 pmol/min/μg, expressed in HEK 293 cells
Synonym(s):
GELB, GELBCLG4B, Gelatinase, Gelatinase B, MANDP2, MMP-9, Matrix Metalloproteinase-10, Type IV collagenase
About This Item
Recommended Products
biological source
human
Quality Level
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
≥50 μg/mL
UniProt accession no.
application(s)
cell analysis
shipped in
dry ice
1 of 4
This Item | PHR2688 | PHR3017 | PHR2796 |
---|---|---|---|
grade certified reference material, pharmaceutical secondary standard | grade certified reference material, pharmaceutical secondary standard | grade certified reference material, pharmaceutical secondary standard | grade certified reference material, pharmaceutical secondary standard |
form solid | form powder | form - | form - |
application(s) pharmaceutical small molecule | application(s) pharmaceutical small molecule | application(s) pharmaceutical | application(s) pharmaceutical small molecule |
API family rocuronium | API family cetrimonium | API family ipratropium | API family - |
packaging pkg of 500 mg | packaging pkg of 1000 mg | packaging pkg of 25 mg | packaging pkg of 400 mg |
General description
Biochem/physiol Actions
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
Physical form
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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