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Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are a family of zinc-dependent proteolytic enzymes that degrade various proteins in the extracellular matrix (ECM). MMPs belong to the large metzincin superfamily of metalloproteases, like the astacins, serralysins, reprolysins, and adamalysins or disintegrin metalloproteinases (ADAMs). MMPs are encoded by 24 human (including a duplicated MMP-23 gene) and 23 mouse genes. The MMP family can be divided into at least six subfamilies: (1) collagenases; (2) gelatinases, (3) stromelysins, (4) matrilysins, (5) MMP membrane-type (MT)-MMPs, and (6) other MMPs. A typical MMPs consists of an N-terminal zymogenic propeptide domain (~80 amino acids), a metal-dependent catalytic domain (~170 amino acids), a linker region (~15-65 amino acids), and a C-terminal hemopexin-like domain (~200 amino acids). All MMPs are synthesized as proenzymes and require a proteolytic cleavage under physiological conditions to promote the release of the propeptide domain (zymogen activation) and generate mature MMPs. MMPs play a central role in many biological processes, such as embryogenesis, normal tissue remodeling, wound healing, and angiogenesis, and in diseases such as atheroma, arthritis, cancer, and tissue ulceration.
rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa Gelatinase; Gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A
Human
HEK293
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Human (HEK293, His) is the recombinant human-derived MMP-2 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MMP-2 Protein, Human (HEK293, His) is 631 a.a., with molecular weight of 68-78 kDa.
72 kDa Type IV Collagenase; Gelatinase A; MMP-2; TBE-1; CLG4A
Human
HEK293
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Human (HEK293) is the recombinant human-derived MMP-2 protein, expressed by HEK293 , with tag free.
MMP-9 is an important member of the MMP protein family and regulates the extracellular matrix during physiological processes such as development and tissue remodeling. It involves arthritis and metastasis. MMP-9 Protein, Human (HEK293) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with tag free. The total length of MMP-9 Protein, Human (HEK293) is 688 a.a., with molecular weight of 80-95 kDa.
The Stromelysin-1/MMP-3 protein is a multifunctional metalloprotease that degrades a variety of extracellular matrix components and activates molecules such as growth factors, plasminogen, and MMP9. It is released into the ECM and is activated through the plasmin cascade. Stromelysin-1/MMP-3 Protein, Human is the recombinant human-derived Stromelysin-1/MMP-3 protein, expressed by E. coli , with tag free. The total length of Stromelysin-1/MMP-3 Protein, Human is 255 a.a., with molecular weight of ~34 kDa.
MMP-8, also known as matrix metalloproteinase-8 or collagenase-2, is recognized for its enzymatic abilities, particularly its ability to break down fibrillar types I, II, and III collagen. This enzymatic activity suggests that MMP-8 plays an important role in the remodeling and turnover of collagen-rich tissues such as connective tissue, cartilage, and bone. MMP-8 Protein, Human (HEK293) is the recombinant human-derived MMP-8 protein, expressed by HEK293 , with N-Met labeled tag. The total length of MMP-8 Protein, Human (HEK293) is 447 a.a., with molecular weight of ~65 kDa.
MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi) is 688 a.a., with molecular weight of 95-105 kDa.
rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa Gelatinase; Gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A
Human
E. coli
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. Animal-Free MMP-2 Protein, Human (His) is the recombinant human-derived animal-FreeMMP-2 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free MMP-2 Protein, Human (His) is 551 a.a., with molecular weight of ~63.00 kDa.
rHuMatrix metalloproteinase-9/MMP-9, His; Matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; MMP9
Human
HEK293
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration. It is suggested that it may be involved in bone osteoclastic resorption. MMP-9 Protein, Human (HEK293, His) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MMP-9 Protein, Human (HEK293, His) is 689 a.a., with molecular weight of ~90.0 kDa.
The MMP-1 protein acts as an enzyme capable of cleaving types I, II, and III collagen at specific sites within the helical domain. In addition, it exhibits lytic activity against type VII and type X collagen. MMP-1 Protein, Human (HEK293, His) is the recombinant human-derived MMP-1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MMP-1 Protein, Human (HEK293, His) is 450 a.a., with molecular weight of 49-61 kDa.
MMP-12 protein is potentially engaged in tissue injury and remodeling, displaying significant elastolytic activity. It shows flexibility at the P1' site, accommodating both large and small amino acids, yet favoring leucine. At the P1 site, it prefers aromatic or hydrophobic residues, with a tendency for small hydrophobic residues like alanine in the P3 position. MMP-12 Protein, Human is the recombinant human-derived MMP-12 protein, expressed by E. coli , with tag free. The total length of MMP-12 Protein, Human is 163 a.a., with molecular weight of ~18 kDa.
Matrix metalloproteinase-9 (Mmp9) is a member of the matrix metalloproteinase (MMP) family. Mmp9 is secreted as inactive proproteins which are activated when cleaved by extracellular proteinases to generate a mature, zinc-dependent endopeptidase enzyme that degrades collagens of type IV, V and XI, and elastin. Mmp9 is also involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow. MMP-9 Protein, Rat (HEK293, His) is the recombinant rat-derived MMP-9 protein, expressed by HEK293 , with C-10*His labeled tag. The total length of MMP-9 Protein, Rat (HEK293, His) is 689 a.a., with molecular weight of approximately 95 kDa.
The MMP-13 protein plays a role in the degradation of extracellular matrix proteins, especially fibrillar collagen, fibronectin, TNC, and ACAN. It cleaves triple-helical collagen, preferentially cleaves type II collagen, and can also target other collagen types. MMP-13 Protein, Human (HEK293) is the recombinant human-derived MMP-13 protein, expressed by HEK293 , with tag free.
rMuMatrix metalloproteinase-9/MMP-9, His; Matrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB
Mouse
HEK293
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration.It is suggested that it may be involved in bone osteoclastic resorption.MMP-9 Protein, Mouse (HEK293, His) is the recombinant mouse-derived MMP-9 protein, expressed by HEK293 , with C-10*His labeled tag.
MMP-8, also known as matrix metalloproteinase-8 or collagenase-2, is recognized for its enzymatic abilities, particularly its ability to break down fibrillar types I, II, and III collagen. This enzymatic activity suggests that MMP-8 plays an important role in the remodeling and turnover of collagen-rich tissues such as connective tissue, cartilage, and bone. MMP-8 Protein, Human (HEK293, His) is the recombinant human-derived MMP-8 protein, expressed by HEK293 , with C-10*His labeled tag. The total length of MMP-8 Protein, Human (HEK293, His) is 447 a.a., with molecular weight of approximately 64.09 kDa.
The Stromelysin-1/MMP-3 protein is a multifunctional metalloprotease that degrades a variety of extracellular matrix components and activates molecules such as growth factors, plasminogen, and MMP9. It is released into the ECM and is activated through the plasmin cascade. Stromelysin-1/MMP-3 Protein, Human (HEK293, His) is the recombinant human-derived Stromelysin-1/MMP-3 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of Stromelysin-1/MMP-3 Protein, Human (HEK293, His) is 460 a.a., with molecular weight of ~60 kDa.
MMP-12 protein has significant elastolytic activity and may contribute to tissue damage and remodeling.Its substrate preferences include preference for leucine at the P1' site and aromatic/hydrophobic residues at the P1 site, and preference for small hydrophobic residues such as alanine at the P3 site.MMP-12 Protein, Mouse (HEK293, His) is the recombinant mouse-derived MMP-12 protein, expressed by HEK293 , with C-6*His labeled tag.
Oma1 protein is an important metalloprotease in the inner mitochondrial membrane that is activated in response to stressors and cleaves targets such as OPA1, UQCC3, and DELE1. Under conditions of loss of membrane potential, Oma1 cleaves OPA1, thereby negatively regulating fusion. OMA1 Protein, Human (Cell-Free, His-SUMO) is the recombinant human-derived OMA1 protein, expressed by E. coli Cell-free , with N-His, N-SUMO labeled tag.
72 kDa Type IV Collagenase; Gelatinase A; MMP-2; TBE-1; CLG4A
Mouse
HEK293
MMP-2 protein is a ubiquitous metalloprotease that contributes to vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to extracellular matrix degradation, it also targets non-matrix proteins and promotes vasoconstriction. MMP-2 Protein, Mouse (HEK293, His) is the recombinant mouse-derived MMP-2 protein, expressed by HEK293 , with N-His labeled tag.
The MMP-26 protein has broad substrate specificity and hydrolyzes type IV collagen, fibronectin, fibrinogen, β-casein, type I gelatin, and α-1 protease inhibitors. The versatility of this enzyme suggests involvement in the degradation and remodeling of various extracellular matrix components. MMP-26 Protein, Human is the recombinant human-derived MMP-26 protein, expressed by E. coli , with tag free. The total length of MMP-26 Protein, Human is 172 a.a., with molecular weight of ~19 KDa.
MMP-10 protein is a member of the matrix metalloproteinase family and plays a crucial role in extracellular matrix remodeling by promoting the degradation of various substrates. As a protease, MMP-10 is involved in tissue homeostasis, wound healing, and inflammatory responses. MMP-10 Protein, Human (P. pastoris, His) is the recombinant human-derived MMP-10 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of MMP-10 Protein, Human (P. pastoris, His) is 378 a.a., with molecular weight of 45 kDa.
