Product Name :
MMP-2 (catalytic domain) (human), (recombinant)
Sequence:
Purity:
≥90% (SDS-PAGE)
Molecular Weight:
~40kDa
Solubility :
Appearance:
Use/Stability :
The enzyme is stable on ice for at least several hours. However, it is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. After initial defrost, aliquot product into individual tubes and refreeze at -70°C. Avoid repeated freeze/defrost cycles.NOTE: When stored under the above conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.
Description:
Represents a naturally occurring active form of MMP-2 which lacks the C-terminal hemopexin domain. MMPs lacking this domain cannot cleave native collagens; however, activity toward other targets such as gelatin, casein, or peptide substrates is unaffected.
CAS :
Solubility:
Formula:
Additional Information :
| Activity Preincubation of MMP-2 catalytic domain at 5nM with the broad-spectrum inhibitor GM6001 at 30nM for 1 hour completely inhibits enzymatic activity.{{2519537-70-1} MedChemExpress|{2519537-70-1} Biological Activity|{2519537-70-1} Formula|{2519537-70-1} custom synthesis} | Alternative Name Matrix metalloproteinase 2, Gelatinase A, 72 kDa Type IV collagenase | Application Notes Useful tool to study enzyme kinetics, cleave target substrates, and screen for inhibitors.{{1009298-09-2} MedChemExpress|{1009298-09-2} Technical Information|{1009298-09-2} Formula|{1009298-09-2} supplier} | Formulation Liquid.PMID:30725752 In 50mM TRIS-HCl, pH 7.5, containing 300mM NaCl, 5mM CaCl2, 20µM ZnCl2, 0.05% Brij-35 and 20% glycerol. | Gene/Protein Identifier NM_004530 (RefSeq) | MW ~40kDa | Purity ≥90% (SDS-PAGE) | Purity Detail Purified by multi-step chromatography. | Source Produced in yeast. Active recombinant matrix metalloproteinase-2 (MMP-2, gelatinase A, 72kDa type IV collagenase) cloned from human cDNA. The enzyme consists of residues Tyr110-Asp452, which comprises the catalytic/fibronectin domain of human MMP-2, with a C-terminal purification tag. | Specific Activity ≥200 pmol/min/µg at 37°C using the colorimetric thiopeptolide Ac-Pro-Leu-Gly-S-Leu-Leu-Gly-OEt (100 µM; Prod. No. BML-P125) as substrate. | UniProt ID P08253
