MMP9 Mouse

Matrix Metalloproteinase-9 Mouse Recombinant

Recombinant mouse MMP9, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain. It comprises 717 amino acids (20-730 a.a.) and has a molecular weight of 79.3 kDa. The protein is engineered with a 6-amino acid Histidine tag at the C-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT7741
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered, colorless solution.

MMP 1 Human

Matrix Metalloproteinase-1 Human Recombinant

Recombinant human MMP-1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 393 amino acids (residues 100-469), including a 23-amino acid N-terminal His-tag, and has a molecular weight of 45 kDa.
Shipped with Ice Packs
Cat. No.
BT7829
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

MMP 1 Human, HEK

Matrix Metalloproteinase-1 Human Recombinant, HEK

Recombinant Human MMP-1, produced in HEK293 cells, is a proform of human MMP-1 encompassing amino acids Met1 to Asn469. It is expressed with a polyhistidine tag at the C-terminus and has a molecular weight of 52 kDa. The purification of MMP-1 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7919
Source
HEK293 cells.
Appearance
Clear, colorless solution, sterile-filtered.

MMP 13 Human

Matrix Metalloproteinase-13 Human Recombinant

The MMP-13 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 391 amino acids (specifically, amino acids 104-471), resulting in a molecular weight of 44.7 kDa. This MMP-13 variant includes a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7982
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

MMP 7 Human

Matrix Metalloproteinase-7 Human Recombinant

Recombinant human MMP-7, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 174 amino acids (residues 95-267). It has a molecular weight of 19.2 kDa. The purification of MMP-7 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8275
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MMP 7 Human, Active

Matrix Metalloproteinase-7 Human Recombinant, Active

Recombinant Matrix Metalloproteinase-7, expressed in E. coli, is produced as a single, non-glycosylated polypeptide chain with a molecular weight of 19.13 kDa. The purification of MMP-7 is achieved through proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT8353
Source
Escherichia Coli.
Appearance
A clear, sterile liquid solution.

MMP9 Human, HEK

Matrix Metalloproteinase-9 Human Recombinant, HEK

This product consists of a recombinant human MMP9 protein, modified to include a 6-amino acid His tag at its C-terminus. The protein is glycosylated and has a molecular weight of 77.2 kDa.
Shipped with Ice Packs
Cat. No.
BT9516
Source

HEK293 Cells.

Appearance
White powder, obtained through lyophilization (freeze-drying) after filtration.

MMP9 Mouse

Matrix Metalloproteinase-9 Mouse Recombinant

MMP9 Mouse Recombinant, produced in HEK cells, is a single, glycosylated polypeptide chain containing 717 amino acids (20-730 a.a). It has a molecular mass of 79.3 kDa. The protein is fused to a 6 amino acid His-tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9609
Source

HEK293 Cells. 

Appearance
Clear, sterile-filtered solution.

MMP-2 Human, HEK

Matrix Metalloproteinase-2 Human Recombinant, HEK

Recombinant Human MMP-2, expressed in HEK293 cells, is a precursor form of human MMP-2 encompassing amino acids Ala30 to Cys660. This protein, with a molecular weight of 71 kDa, is engineered with a polyhistidine tag at its C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9176
Source
HEK293 cells.
Appearance
MMP-2 is provided as a clear, sterile solution that has undergone filtration.

MMP2 Mouse

Matrix Metalloproteinase-2 Mouse Recombinant

MMP2 Mouse, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 644 amino acids (residues 30-662). It has a molecular weight of 72.4 kDa. The protein features a 6-amino acid Histidine tag fused to its C-terminus. Purification is achieved using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9245
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Definition and Classification

Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are a family of calcium-dependent zinc-containing endopeptidases. They belong to the larger metzincin superfamily of proteases . MMPs are classified based on their substrate specificity and domain structure into several groups: collagenases, gelatinases, stromelysins, matrilysins, and membrane-type MMPs (MT-MMPs) .

Biological Properties

MMPs are known for their ability to degrade various components of the extracellular matrix (ECM), but they also play roles in regulating extracellular tissue signaling networks . They are expressed in various tissues and have distinct expression patterns. For instance, MMP-1 is found in fibroblasts, MMP-2 in endothelial cells, and MMP-9 in neutrophils . Their tissue distribution is broad, encompassing skin, lungs, heart, and other organs .

Biological Functions

MMPs contribute to the homeostasis of many tissues and participate in several physiological processes, such as bone remodeling, angiogenesis, immunity, and wound healing . They play a crucial role in immune responses by regulating the release or activation of chemokines, cytokines, and growth factors . MMPs are also involved in pathogen recognition and host defense mechanisms .

Modes of Action

MMPs interact with other molecules and cells through various mechanisms. They can be activated by chaotropic agents or by cleavage of the pro-peptide by other proteases . MMPs bind to specific substrates and degrade them, influencing cell behaviors such as migration, proliferation, and apoptosis . They also participate in downstream signaling cascades by modulating the availability of growth factors and cytokines .

Regulatory Mechanisms

The activity of MMPs is tightly regulated at multiple levels:

  1. Gene Expression: Transcription and mRNA stability are key regulatory points .
  2. Compartmentalization: This regulates the efficiency of proteolysis through cell surface recruitment and substrate availability .
  3. Pro-enzyme Activation: MMPs are synthesized as inactive zymogens and require activation .
  4. Inhibition: Tissue inhibitors of metalloproteinases (TIMPs) are endogenous inhibitors that regulate MMP activity .
Applications

MMPs have significant applications in biomedical research, serving as diagnostic tools and therapeutic targets. They are involved in the diagnosis and treatment of various diseases, including cancer, arthritis, and cardiovascular diseases . MMP inhibitors are being explored as potential therapeutic agents to modulate MMP activity in pathological conditions .

Role in the Life Cycle

MMPs play essential roles throughout the life cycle, from development to aging and disease. During embryogenesis, they are involved in tissue remodeling and morphogenesis . In adulthood, MMPs contribute to tissue repair and maintenance . Dysregulation of MMP activity is associated with aging and various diseases, including cancer and fibrosis .

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