Recombinant Human MMP9 protein (Active) is a Human Fragment protein, in the 107 to 457 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, FuncS
Yes
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide.
CLG4B, MMP9, CLG4B, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB
Recombinant Human MMP9 protein (Active) is a Human Fragment protein, in the 107 to 457 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
>95% SDS-PAGE
Escherichia coli
His tag N-Terminus
SDS-PAGE, FuncS
Yes
The activity was determined using fluorogenic substrate Mca-PLGL-Dpa-AR-NH2. The specific activity is ≥200 μU/μg.
One unit (U) of the activity is defined as the amount of enzyme that releases 1 μmole of Mca from McaPLGL-Dpa-AR-NH2 per min. at 37°C.
P14780
No
Human
Reconstitute in water, 30% glycerol
Constituents: 32% Trehalose, 9.6% Dextran, 1.2% BSA, 0.59% Potassium chloride, 0.46% Sodium chloride, 0.38% Tripotassium orthophosphate, 0.12% Alcohol Ethoxylate, 0.107% Magnesium acetate, 0.07% EDTA, 0.06% Tris HCl, 0.018% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Fragment
41.3 kDa
107 to 457
Recombinant
His tag N-Terminus
Lyophilized
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide.
Belongs to the peptidase M10A family.
Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This supplementary information is collated from multiple sources and compiled automatically.
The MMP-9 protein also known as matrix metalloproteinase-9 or gelatinase B functions as an enzyme involved in the breakdown of extracellular matrix proteins. It consists of a zinc ion at its active site and facilitates the degradation of type IV and V collagens fibronectin and elastin. MMP-9 has a molecular weight of approximately 92 kDa and is expressed in a variety of tissues including the liver lungs and immune cells. This enzyme can exist in monomer and dimer forms with its activity regulated by tissue inhibitors of metalloproteinases (TIMPs).
Matrix metalloproteinase-9 profoundly influences tissue remodeling inflammation and angiogenesis. It does not form part of a larger protein complex but interacts closely with substrates in the extracellular matrix. MMP-9 plays important roles in processes such as embryogenesis reproduction and wound healing through the remodeling of surrounding tissues. The MMP-9 protein is often measured using assays like ELISA or analyzed via techniques such as Western blotting to determine its expression levels and activity in different biological contexts.
MMP-9 participates in the matrix metalloproteinase pathway and the NF-kB signaling pathway. These pathways are essential in orchestrating processes such as tissue remodeling and inflammatory responses. MMP-9 acts alongside other matrix metalloproteinases including MMP-2 and is regulated by factors like cytokines growth factors and hormones ensuring the precision of extracellular matrix degradation during physiological processes.
Matrix metalloproteinase-9 has associations with cancer invasion and metastasis as well as chronic inflammatory diseases like rheumatoid arthritis. In cancer upregulated MMP-9 expression aids tumor cells in breaching the basement membrane facilitating metastasis. The disorder-associated pathways often involve interactions with proteins like vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta). Understanding MMP-9's role in these conditions can contribute to developing targeted therapies that inhibit its activity potentially mitigating disease progression.
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Terms & Conditions.
MMP-9 was reconstituted in 30% Glycerol/H2O solution and the indicated amount of MMP-9 were incubated with substrate (Mca-PLGL-Dpa-AR-NH2) in a 100 μl Assay Buffer using MMP-9 Inhibitor Screening Kit (MMP-9 Inhibitor Screening Kit (Fluorometric) ab284517). The fluorescence (Ex/Em 325/393 nm) was monitored over a 30 min time period.
SDS-PAGE (4-20%) of Recombinant MMP-9: Recombinant protein loaded under reducing conditions and stained with Coomassie Blue. Lane M-MW marker, Lane 1- 2 μg, Lane 2- 4 μg, Lane 3- 8 μg rhMMP-9.
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