MMP 8 Human

Matrix Metalloproteinase-8 Human Recombinant

Produced in E. coli, Recombinant Human Matrix Metalloproteinase-8 is a single polypeptide chain devoid of glycosylation, possessing a molecular weight of 75 kDa.
The purification of MMP-8 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8425
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

MMP 8 Human, His

Matrix Metalloproteinase-8 Human Recombinant, His Tag

Recombinant human MMP-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 390 amino acids (residues 101-467). It has a molecular weight of 44.3 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT8516
Source
Escherichia Coli.
Appearance
Sterile filtered, colorless solution.

MMP 9 Human

Matrix Metalloproteinase-9 Human Recombinant

Recombinant human MMP-9 is a truncated form of the protein expressed in E. coli. This form comprises the catalytic domain (amino acids 113-450) and a 4.5kDa hexahistidine tag at the N-terminus, resulting in a total molecular weight of 42.03 kDa. The protein is purified using chromatography techniques, resulting in a highly pure preparation.
Shipped with Ice Packs
Cat. No.
BT8570
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

MMP 9 Rabbit

Matrix Metalloproteinase-9 Rabbit Recombinant

This product consists of a recombinant MMP-9 protein derived from rabbits. It encompasses the complete amino acid sequence of the secreted protein, along with a C-terminal Myc-His tag for detection and purification purposes. Produced in insect cells, the recombinant MMP-9 exhibits a molecular weight of approximately 95 kDa due to post-translational modifications.
Shipped with Ice Packs
Cat. No.
BT8645
Source
Baculovirus system, insect cells.
Appearance
The product is a clear solution that has undergone sterile filtration.

MMP1 (24-207) Human

Matrix Metalloproteinase-1 (24-207 a.a) Human Recombinant, HEK

MMP1 (24-207) Human Recombinant is a single-chain polypeptide that has been glycosylated. It encompasses amino acids 24 to 207 of the MMP-1 protein, resulting in a molecular mass of 21.2 kDa. This recombinant protein also includes a 6-amino acid His tag attached to its C-terminus.
Shipped with Ice Packs
Cat. No.
BT8721
Source

HEK293 Cells.

Appearance
White powder, obtained through filtration and lyophilization.

ProMMP 9 Human

Pro-Matrix Metalloproteinase-9 Human Recombinant

Recombinant human Pro-MMP-9, produced in E. coli, is a non-glycosylated polypeptide chain consisting of 688 amino acids (fragment 20-707). This fragment corresponds to the pro-form of MMP-9 without the signal peptide. It has a molecular mass of 78.59 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag. The purification of Pro-MMP-9 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9894
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

MMP9 Human, Sf9

Matrix Metalloproteinase-9 Human Recombinant, Sf9

Recombinant human MMP9, expressed in Sf9 insect cells, is a single, glycosylated polypeptide chain consisting of 694 amino acids (20-707a.a.). With a molecular weight of 77.1 kDa, it appears as a band at approximately 70-100 kDa on SDS-PAGE. The protein features a 6-amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT7659
Source

Sf9, Baculovirus cells.

Appearance
Sterile, colorless solution.

MMP 3 Human

Matrix Metalloproteinase-3 Human Recombinant

Recombinant human MMP-3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 401 amino acids (residues 100-477). It has a molecular weight of 45.2 kDa. The protein includes a 23-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8069
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MMP 3 Human, GST

Matrix Metalloproteinase-3 Human Recombinant, GST Tag

Recombinant human MMP-3, expressed in E. coli, is a monomeric protein. It consists of a single polypeptide chain devoid of glycosylation. The protein includes a GST tag and comprises 228 amino acids (residues 251-478), resulting in a molecular weight of 51 kDa. The purification of MMP-3 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8147
Source
Escherichia Coli.
Appearance
Clear solution, sterile-filtered.

MMP 3 Human, HEK

Matrix Metalloproteinase-3 Human Recombinant, HEK

Recombinant Human MMP-3, produced in HEK293 cells, is a proform of human MMP3 [Tyr18-Cys477 (Lys45Glu)] with a polyhistidine tag at the C-terminus, resulting in a molecular weight of 52kDa. This protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8202
Source
HEK293 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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