Native Human MMP-9/Lipocalin/TIMP-1 Complex
Cat.No. : | MMP9-40H |
Product Overview : | Matrix Metalloproteinase 9–Lipocalin–TIMP-1 complex, Gelatinase B, 92-kDa Type IV Collagenase, EC 3.4.24.35). Prepared from human blood certified to be negative for HBsAg and for antibodies to HIV and HCV. |
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Source : | Human neutrophil granulocytes (Buffy Coat) |
Species : | Human |
Form : | Liquid, in 50 mM Tris/HCl, pH 7.0, 200 mM NaCl, 5 mM CaCl2, 1 μM ZnCl2, 0.05% NaN3, 0.05% Brij 35. |
Purity : | >95%, homogenous by electrophoresis and Western Blotting analysis |
Unit Definition : | The specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-petide) (Masui et al. 1977). One unit MMP catalyzes the hydrolysis of 1 μmol Dnp peptide/min at 37°C and pH 7.0. |
Storage : | The enzyme is very stable if stored at -80°C. Repeated freezing and thawing must be avoided. |
Tag : | Non |
Gene Name : | MMP9 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) [ Homo sapiens ] |
Official Symbol : | MMP9 |
Synonyms : | MMP9; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); CLG4B, matrix metalloproteinase 9 (gelatinase B, 92kD gelatinase, 92kD type IV collagenase) , matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase-9; 92 kDa gelatinase; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); GELB; CLG4B; MMP-9; MANDP2; |
Gene ID : | 4318 |
mRNA Refseq : | NM_004994 |
Protein Refseq : | NP_004985 |
MIM : | 120361 |
UniProt ID : | P14780 |
Chromosome Location : | 20q12-q13 |
Pathway : | Activation of Matrix Metalloproteinases, organism-specific biosystem; Bladder cancer, organism-specific biosystem; Bladder cancer, conserved biosystem; CXCR4-mediated signaling events, organism-specific biosystem; Degradation of the extracellular matrix, organism-specific biosystem; Endochondral Ossification, organism-specific biosystem; Extracellular matrix organization, organism-specific biosystem; |
Function : | collagen binding; fibronectin binding; metal ion binding; metalloendopeptidase activity; peptidase activity; protein binding; protein complex binding; zinc ion binding; |
Products Types
◆ Recombinant Protein | ||
MMP9-5438H | Recombinant Human MMP9 Protein, GST-tagged | +Inquiry |
Mmp9-10596M | Recombinant Mouse Mmp9 Protein, His (Fc)-Avi-tagged | +Inquiry |
MMP9-6754H | Recombinant Horse MMP9 protein | +Inquiry |
MMP9-1129H | Recombinant Human MMP9 Protein, His-tagged | +Inquiry |
MMP9-03H | Active Recombinant Pre-activated Human MMP9 Protein | +Inquiry |
◆ Native Protein | ||
MMP9-41H | Native Human MMP-9/TIMP-1 Complex | +Inquiry |
MMP9-29698TH | Native Human MMP9 | +Inquiry |
MMP9-30035TH | Native Human MMP9 | +Inquiry |
◆ Lysates | ||
MMP9-2560HCL | Recombinant Human MMP9 cell lysate | +Inquiry |
MMP9-1940RCL | Recombinant Rat MMP9 cell lysate | +Inquiry |
MMP9-2026MCL | Recombinant Mouse MMP9 cell lysate | +Inquiry |
◆ Assay kits | ||
Kit-2130 | MMP-9 Inhibitor Screening Kit | +Inquiry |
Kit-3100 | MMP-9 Fluorimetric Assay Kit | +Inquiry |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewThe superior quality of this recombined protein has significantly enhanced the precision of our research outcomes.
Fast shipping! Ordered this product, and it arrived well-packaged and ready for use in our experiments.
Customer service went above and beyond to accommodate our specific needs, ensuring a smooth purchasing experience.
Q&As (5)
Ask a questionDysregulated MMP9 expression is associated with cancer invasion and metastasis, as it enables tumor cells to degrade the extracellular matrix and invade surrounding tissues.
Polymorphisms in the MMP9 gene can influence enzyme activity, potentially affecting the individual's susceptibility to certain diseases and the progression of pathological conditions.
MMP9 facilitates tissue remodeling by cleaving structural proteins in the extracellular matrix, such as collagen and gelatin, leading to changes in tissue architecture.
MMP9 contributes to the breakdown of the blood-brain barrier by degrading tight junction proteins, potentially exacerbating neurological disorders and neuroinflammation.
MMP9 plays a role in angiogenesis by promoting the release and activation of growth factors sequestered in the extracellular matrix, facilitating the formation of new blood vessels.
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