Recombinant human MMP2 protein (Active) is a Human Full Length protein, in the 109 to 660 aa range, expressed in Escherichia coli, with >98%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC, FuncS.
View Alternative Names
CLG4A, MMP2, 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, TBE-1, MMP-2
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Matrix metalloproteinase-2 is mainly involved in the degradation of type IV and V collagens gelatin and fibronectin. As part of the metalloproteinase family it works alongside other MMPs to maintain tissue homeostasis and repair. MMP-2 forms part of a complex network that ensures the timely degradation of matrix components balancing synthesis and breakdown. It remains regulated by tissue inhibitors of metalloproteinases (TIMPs) preventing excessive degradation that could lead to tissue damage.
Pathways
MMP-2 plays a significant role within the extracellular matrix (ECM) remodeling and angiogenesis pathways. It interacts with various proteins including integrins and TIMP-2 to modulate cellular behaviors such as migration and invasion. MMP-2 contributes to processes like wound healing and embryonic development through its involvement in ECM degradation and new tissue formation.
Specifications
Form
Lyophilized
Additional notes
>= 98% HPLC.
General info
Function
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.. PEX, the C-terminal non-catalytic fragment of MMP2, possesses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.. Isoform 2. Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
Sequence similarities
Belongs to the peptidase M10A family.
Post-translational modifications
Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.. The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.
Subcellular localisation
Mitochondrion
Target data
Publications (10)
Recent publications for all applications. Explore the full list and refine your search
Scientific reports 13:19227 PubMed37932474
2023
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Frontiers in pharmacology 14:1215694 PubMed37492088
2023
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Science advances 9:eabq8225 PubMed36857458
2023
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BMC cancer 22:1335 PubMed36539774
2022
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Scientific reports 12:14462 PubMed36002564
2022
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International journal of molecular sciences 22: PubMed34070317
2021
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Scientific reports 9:4340 PubMed30867536
2019
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International journal of molecular sciences 19: PubMed29463024
2018
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Mediators of inflammation 2017:9524594 PubMed29097850
2017
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Biochimica et biophysica acta. Molecular basis of 1863:2808-2820 PubMed28712835
2017
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