Abcam, ab39309, Recombinant Mouse MMP9 protein

Size: 10µg
Recombinant Mouse MMP9 protein is a Mouse Full Length protein, expressed in BHK cells, with 95%, suitable for SDS-PAGE, WB, FuncS.
Key facts
Purity:95%,
Expression system:BHK cells,
Tags:Tag free,
Applications:FuncS, SDS-PAGE, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P41245,
Animal free:No,
Carrier free:No,
Species:Mouse,
Storage buffer:pH: 7.4Constituents: PBS, 50% Glycerol (glycerin, glycerine), 1.45% Sodium chloride

Product details:
Mouse-MMP9 degrades denatured collagen (gelatin), and a range of extracellular matrix components in-vivo. Unlike MMP2, MMP9 is not constituitively produced by most normal cells, although the enzyme is often over expressed by transformed cells, tumor cells, and cells treated with the phorbol ester PMA. An endogenous inhibitor to MMP9, TIMP1, is often complexed with the enzyme in-vivo, but has been removed from this preparation.
ab39309 is a mix of active and latent enzymes, approximately 25% active.
For Gelatin zymography the MMP9 does not need to be pre-activated, the SDS in the sample buffer will activate the enzyme sufficiently. For any other assays, or to get maximum activity the MMP9 will need activation, as is is mostly in latent form. APMA at 1 mM works, in a buffer of PBS with 10 mM CaCl
, 100 μM ZnCl
, and 0.05% Brij-35, 37°C for a minimum of 1 hour.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
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).
Biological function summary
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.
Pathways
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.