Recombinant human MMP9 protein (Proenzyme)
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(1 Publication)
Recombinant human MMP9 protein (Proenzyme) is a Human Fragment protein, in the 20 to 469 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.
View Alternative Names
CLG4B, MMP9, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human MMP9 protein (Proenzyme) (AB155704)
Purity of ab155704 determined by SDS-PAGE under reduced conditions and stained overnight with Coomassie Blue
Complementary Products
Reactivity data
Product details
*100mM APMA stock solution should be prepared in DMSO. Please avoid adding high concentration APMA solution (>20mM) directly into the reaction as it tends to precipitate. A pre-dilution step is highly recommended.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Lyophilized
Additional notes
Purified by Immobilized metal affinity chromatography.
General info
Function
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.
Sequence similarities
Belongs to the peptidase M10A family.
Post-translational modifications
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.. N- and O-glycosylated.
Target data
Publications (1)
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Nature communications 14:801 PubMed36781854
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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