Recombinant human MMP2 protein (Active) is a Human Full Length protein, in the 109 to 660 aa range, expressed in Escherichia coli, with >=98% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
M Y N F F P R K P K W D K N Q I T Y R I I G Y T P D L D P E T V D D A F A R A F Q V W S D V T P L R F S R I H D G E A D I M I N F G R W E H G D G Y P F D G K D G L L A H A F A P G T G V G G D S H F D D D E L W T L G E G Q V V R V K Y G N A D G E Y C K F P F L F N G K E Y N S C T D T G R S D G F L W C S T T Y N F E K D G K Y G F C P H E A L F T M G G N A E G Q P C K F P F R F Q G T S Y D S C T T E G R T D G Y R W C G T T E D Y D R D K K Y G F C P E T A M S T V G G N S E G A P C V F P F T F L G N K Y E S C T S A G R S D G K M W C A T T A N Y D D D R K W G F C P D Q G Y S L F L V A A H E F G H A M G L E H S Q D P G A L M A P I Y T Y T K N F R L S Q D D I K G I Q E L Y G A S P D I D L G T G P T P T L G P V T P E I C K Q D I V F D G I A Q I R G E I F F F K D R F I W R T V T P R D K P M G P L L V A T F W P E L P E K I D A V Y E A P Q E E K A V F F A G N E Y W I Y S A S T L E R G Y P K P L T S L G L P P D V Q R V D A A F N W S K N K K T Y I F A G D K F W R Y N E V K K K M D P G F P K L I A D A W N A I P D N L D A V V D L Q G G G H S Y F F K G A Y Y L K L E N Q S L K S V K F G S I K S D W L G C
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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.
CLG4A, MMP2, 72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, TBE-1, MMP-2
Recombinant human MMP2 protein (Active) is a Human Full Length protein, in the 109 to 660 aa range, expressed in Escherichia coli, with >=98% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
At an MMP2 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.
>= 98% HPLC.
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.
Belongs to the peptidase M10A family.
Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
The MMP-2 protein also known as matrix metalloproteinase-2 or gelatinase A is an enzyme involved in the breakdown of extracellular matrix components. It plays a critical role in tissue remodeling and cell migration. Comprised of a molecular weight of approximately 72 kDa this metalloproteinase is secreted as an inactive proenzyme that requires activation. MMP2 is expressed in various tissues including the brain heart and blood vessels where it contributes to normal physiological processes and pathological conditions.
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.
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.
Matrix metalloproteinase-2 is linked to cancer progression and cardiovascular diseases. In cancer abnormal MMP-2 activity facilitates tumor invasion and metastasis by breaking down matrix barriers. Increased MMP-2 expression associates with poor prognosis in cancers like breast and prostate. In cardiovascular diseases such as atherosclerosis it contributes to plaque destabilization and vascular remodeling. The imbalance in MMP-2 activity and its regulation by proteins like TIMP-1 are involved in the pathology of these disorders.
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