MMP 8 Human

Matrix Metalloproteinase-8 Human Recombinant

Matrix Metalloproteinase-8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 75 kDa.
The MMP-8 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8425
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MMP 8 Human, His

Matrix Metalloproteinase-8 Human Recombinant, His Tag

MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8516
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

MMP 9 Human

Matrix Metalloproteinase-9 Human Recombinant

MMP-9 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 338 amino acids fragment (113-450) corresponding to the catalytic domain of the protein, having a total molecular mass of 42.03kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The MMP-9 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8570
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MMP 9 Rabbit

Matrix Metalloproteinase-9 Rabbit Recombinant

MMP-9 Rabbit Recombinant is a full length secreted protein (688 amino acids - a.a. 20-707). The MMP-9 is expressed in insect cells and fused to a 30 aa C-terminal Myc-His tag, having a total MW of 79.94kDa. Purified MMP9 protein appears at 95kDa on SDS-PAGE gel due to protein modification.
Shipped with Ice Packs
Cat. No.
BT8645
Source
Baculovirus system, insect cells.
Appearance
Sterile Filtered clear solution.

MMP1 (24-207) Human

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

MMP1 (24-207) Human Recombinant is a single, glycosylated polypeptide chain containing 190 amino acids and having a molecular mass of 21.2kDa. MMP1 (24-207) is fused to a 6 a.a C-terminal His tag.  

Shipped with Ice Packs
Cat. No.
BT8721
Source

HEK293 Cells.

Appearance
Filtered White lyophilized (freeze-dried) powder.

MMP1 Human, sf9

Matrix Metalloproteinase-1 Human Recombinant, sf9

MMP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 460 amino acids (18-469a.a) and having a molecular mass of 53.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). 
MMP1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8799
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

MMP10 Human

Matrix Metallopeptidase 10 Human Recombinant

MMP10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (99-476a.a) and having a molecular mass of 45.4kDa. MMP10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8870
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

MMP14 Human

Matrix Metalloproteinase-14 Recombinant Human

Matrix Metalloproteinase-14 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 264 amino acids and having a molecular mass of 29.6kDa.

MMP14 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8950
Source

Escherichia Coli.

Appearance

Sterile filtered colorless solution.

MMP14 Human, His

Matrix Metalloproteinase-14 Human Recombinant, His Tag

MMP14 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 527 amino acids (21-538a.a) and having a molecular mass of 59.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-70kDa). 
MMP14 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9004
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

MMP2 Human

Matrix Metalloproteinase-2 Human Recombinant

MMP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 576 amino acids (110-660a.a) and having a molecular mass of 64.7kDa. MMP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9093
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
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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