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Active Recombinant Human MMP9

Cat.No. : MMP9-166H
Product Overview : Active recombinant matrix metalloproteinase-9 (MMP-9, gelatinase B, 92 kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Phe107-Pro449 (NM_004994), which comprises the catalytic/fibronectin domain of human MMP-9, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-9 which lacks the C-terminal hemopexin domain. Activity toward its targets, such as gelatin, casein, or peptide substrates, is unaffected.
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Description : Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP''s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Source : E. coli
Species : Human
Form : Liquid. In 50mM TRIS, pH 7.5, containing 5mM calcium chloride, 300mM sodium chloride, 20µM zinc chloride, 0.5% Brij-35 and 30% glycerol.
Bio-activity : XX U/µg. One U=100pmol/min at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt as substrate. Preincubation of MMP-9 catalytic domain at 1.3nM with the broad-spectrum inhibitor GM6001 at 30nM for 1 hour inhibits enzymatic activity by 97%.
Molecular Mass : 39 kDa
Purity : ≥95% (SDS-PAGE)
Applications : Study enzyme kinetics, cleave target substrates, and screen for inhibitors.
Storage : -80°C
Concentration : 0.5µg/µl
Gene Name : MMP9 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) [ Homo sapiens (human) ]
Official Symbol : MMP9
Synonyms : MMP9; GELB; CLG4B; MMP-9; MANDP2; matrix metallopeptidase 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); EC 3.4.24.35
Gene ID : 4318
mRNA Refseq : NM_004994
Protein Refseq : NP_004985
MIM : 120361
UniProt ID : P14780
Chromosome Location : 20q11.2-q13.1
Pathway : AGE/RAGE pathway; Angiogenesis; Bladder cancer
Function : collagen binding; metalloendopeptidase activity; protein binding

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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What are the consequences of dysregulated MMP9 expression in cancer progression? 02/13/2022

Dysregulated MMP9 expression is associated with cancer invasion and metastasis, as it enables tumor cells to degrade the extracellular matrix and invade surrounding tissues.

What is the impact of MMP9 polymorphisms on enzyme activity? 09/07/2021

Polymorphisms in the MMP9 gene can influence enzyme activity, potentially affecting the individual's susceptibility to certain diseases and the progression of pathological conditions.

Can you explain the role of MMP9 in tissue remodeling at the molecular level? 01/17/2020

MMP9 facilitates tissue remodeling by cleaving structural proteins in the extracellular matrix, such as collagen and gelatin, leading to changes in tissue architecture.

What is the role of MMP9 in the breakdown of the blood-brain barrier during neurological disorders? 11/14/2019

MMP9 contributes to the breakdown of the blood-brain barrier by degrading tight junction proteins, potentially exacerbating neurological disorders and neuroinflammation.

How does MMP9 contribute to angiogenesis at the molecular level? 06/02/2018

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.

Customer Reviews (3)

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Reviews
05/03/2020

    The superior quality of this recombined protein has significantly enhanced the precision of our research outcomes.

    08/15/2019

      Fast shipping! Ordered this product, and it arrived well-packaged and ready for use in our experiments.

      01/21/2018

        Customer service went above and beyond to accommodate our specific needs, ensuring a smooth purchasing experience.

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