Application Note
MMP9 is a zinc-dependent enzymes capable of cleaving components of the extracellular matrix, which belongs to the matrix metalloproteinase (MMP) family. It is a gelatinase A, 92kDa type IV collagenase which can hydrolyze gelatin under certain conditions. Gelatin zymography is mainly used for the detection of the gelatinases, MMP-2 and MMP-9, and it is extremely sensitive because levels of 10pg of MMP-2 can already be detected. Briefly, various concentrations of recombinant human MMP9 (1000ng, 500ng, 100ng, 10ng) were denatured by SDS loading buffer, electrophoresed through sodium dodecylsulphate- polyacrylamide gel (SDS-PAGE; 10% gels) containing gelatin (1 mg/ml) with nonreducing conditions. After renaturation, incubation and CCB-stained, active MMP2 would hydrolyze gelatin nearby, which was indicated by the white binds on the gel. In this experiment we use heat-denatured MMP9 protein as negative control, and blood sample as positive control.
Form
Lyophilized powder
Buffer
Reconstitute with 20mM Tris (pH8.0) and 150mM NaCl to 0.1-1.0mg/ml. Do not vortex. Lyophilized from 20mM Tris (pH8.0), 150mM NaCl, 1mM EDTA, 1mM DTT, 0.01% SKL, 5% Trehalose.
Preservative
ProClin 300
Storage
For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, store at -20ºC or below. After reconstitution, keep as concentrated solution. Avoid freeze-thaw cycles.
Region/Sequence
N-terminal His-Tagged; Gly213-Ala399
Expression System
E. coli
Purity
> 95%
Endotoxin
< 1.0 EU per μg (determined by the LAL method)
Conjugation
Unconjugated
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
matrix metallopeptidase 9 , CLG4B , GELB , MANDP2 , MMP-9
Background
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. [provided by RefSeq, Jul 2008]
Database
Research Area