Loading...
You have changed your country from
to
. Please be aware that this will change the currency in the purchasing process.
Products:Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
Overview
Product name
MMP9 protein (Human)
See all MMP9 products (12) ...
Protein description
Pro-MMP9 from cell culture media of stimulated human fibroblasts.
Properties
Purification notes
Purified from cell culture media of stimulated human fibroblasts, this protein is free of its endogenous inhibitor, TIMP1, and other matrix metalloproteinases.
Form
Liquid
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage buffer
Preservative: None
Constituents: 50% Glycerol, PBS, 250mM Sodium chloride, pH 7.4
Concentration
Concentration information loading...
Research areas
Cardiovascular >> Atherosclerosis >> Thrombosis >> Other
Cancer >> Tumor biomarkers >> Enzymes >> MMPs
Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> MMPs
Cancer >> Invasion/microenvironment >> ECM >> Extracellular matrix >> MMPs
Cancer >> Invasion/microenvironment >> Angiogenesis >> ECM enzymes >> MMPs
Signal Transduction >> Cytoskeleton / ECM >> Extracellular Matrix >> ECM Enzymes >> MMP
Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP
Applications
Show applications key
Our Abpromise guarantee covers the use of ab39308 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
FuncS: Use at an assay dependent dilution. (PubMed: 20422465Attenuation of the voltage-induced contraction of mouse primary cardiomyocytes.)
SDS-PAGE: Use at an assay dependent dilution.
WB: Use at an assay dependent dilution. Predicted molecular weight: 92 kDa.(Use at an assay dependent dilution. Predicted molecular weight: 92 kDa. Dilution optimised using Chromogenic detection. This enzyme is supplied predominantly as a zymogen, with a small amount of processed (cleaved) enzyme present. The zymogen can be activated by incubation at 37 degree Celsius for 2 to 6 hours with the organomercurial compound APMA at 1 mM. The enzyme degrades denatured collagen (gelatin), and a range of extracellular matrix components in vivo.)
Protein info
Function
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-
-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Tissue specificity
Produced by normal alveolar macrophages and granulocytes.
Involvement in disease
Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [MIM:603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain.
Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [MIM:613073]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
Sequence similarities
Belongs to the peptidase M10A family.
Contains 3 fibronectin type-II domains.
Contains 4 hemopexin-like domains.
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
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.
Cellular localization
Secreted > extracellular space > extracellular matrix.
Target information above from: UniProt accessionP14780
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010).
References for MMP9 protein (Human) (ab39308)
This product has been referenced in:
- Mishra PKet al. MMP-9 gene ablation and TIMP-4 mitigate PAR-1-mediated cardiomyocyte dysfunction: a plausible role of dicer and miRNA. Cell Biochem Biophys 57:67-76 (2010). Functional Studies.Read more (PubMed: 20422465) »
- Sans-Fons MGet al. Matrix metalloproteinase-9 and cell division in neuroblastoma cells and bone marrow macrophages. Am J Pathol 177:2870-85 (2010). Functional Studies.Read more (PubMed: 20971732) »
See all 2 publications for this product
Publishing research using ab39308? Please let us know so that we can cite the reference in this datasheet
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"