MMP2
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
> 90 % as determined by SDS-PAGE and Coomassie blue staining
Func, AbP, STD, PI
Active
Functional Studies (Func), Antibody Production (AbP), Standard (STD), Protein Interaction (PI)
Specificité
Optimal preservation of protein structure, post-translational modifications and functions.
Attributs du produit
Recombinant human MMP-2 (transcript variant 1) protein expressed in E. coli.
Produced with end-sequenced ORF clone
Tested for bioactivity.
Pureté
> 90 % as determined by SDS-PAGE and Coomassie blue staining
niveau d'endotoxine
Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).
Biological Activity Comment
MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 ug/mL, 50% cleavage was achieved at an incubation time of approximately 25 minutes.
Crystallography grade
MMP2
Origine: Souris
Hôte: Cellules d'insectes
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA, Crys
Indications d'application
Recombinant human proteins can be used for: Native antigens for optimized antibody production Positive controls in ELISA and other antibody assays Protein-protein interaction In vitro biochemical assays and cell-based functional assays
Restrictions
For Research Use only
Buffer
Lyophilized from a 0.2 μM filtered solution of 20 mM phosphate buffer,100 mM NaCl, pH 7.2
Conseil sur la manipulation
Resuspend the protein in the desired concentration in proper buffer
Stock
-80 °C
Stockage commentaire
Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
This gene is a member of the matrix metalloproteinase (MMP) gene family, that are zinc-dependent enzymes capable of cleaving components of the extracellular matrix and molecules involved in signal transduction. The protein encoded by this gene is a gelatinase A, type IV collagenase, that contains three fibronectin type II repeats in its catalytic site that allow binding of denatured type IV and V collagen and elastin. Unlike most MMP family members, activation of this protein can occur on the cell membrane. This enzyme can be activated extracellularly by proteases, or, intracellulary by its S-glutathiolation with no requirement for proteolytical removal of the pro-domain. This protein is thought to be involved in multiple pathways including roles in the nervous system, endometrial menstrual breakdown, regulation of vascularization, and metastasis. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms.