Recombinant Human MMP-2/CLG4A protein (His Tag) (PDEH100909)

For research use only.
Synonyms | 72 kDa Gelatinase, 72 kDa Type IV Collagenase, CLG4, CLG4A, Gelatinase A, MMP-2, MMP-II, MMP2, MONA, Matrix Metalloproteinase-2, TBE-1 |
Species | Human |
Expression Host | E.coli |
Sequence | Lys359-Cys660 |
Accession | P08253 |
Calculated Molecular Weight | 33.1 kDa |
Observed Molecular Weight | 38 kDa |
Tag | N-His |
Bio-activity | Not validated for activity |
Purity | > 95% as determined by reducing SDS-PAGE. |
Endotoxin | < 10 EU/mg of the protein as determined by the LAL method |
Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol. |
Reconstitution | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis. |
Background | 72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.It belongs to the matrix metalloproteinase (MMP) family. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP-2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways. |
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