MMP9 Human, Sf9

Matrix Metalloproteinase-9 Human Recombinant, Sf9

MMP9 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing  694 amino acids (20-707a.a.) and having a molecular mass of  77.1 kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7659
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

MMP9 Mouse

Matrix Metalloproteinase-9 Mouse Recombinant

MMP9 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing  717 amino acids (20-730 a.a.) and having a molecular mass of  79.3 kDa. MMP9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT7741
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

MMP 1 Human

Matrix Metalloproteinase-1 Human Recombinant

MMP 1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (100-469a.a) and having a molecular mass of 45kDa. MMP 1 is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT7829
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

MMP 1 Human, HEK

Matrix Metalloproteinase-1 Human Recombinant, HEK

MMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa.
MMP-1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7919
Source
HEK293 cells.
Appearance
Sterile Filtered colorless solution.

MMP 13 Human

Matrix Metalloproteinase-13 Human Recombinant

MMP-13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT7982
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MMP 3 Human

Matrix Metalloproteinase-3 Human Recombinant

MMP 3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (100-477a.a) and having a molecular mass of 45.2kDa.
MMP 3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8069
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

MMP 3 Human, GST

Matrix Metalloproteinase-3 Human Recombinant, GST Tag

MMP-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain fused to a GST tag containing 228 amino acids (251-478) and having a total molecular mass of 51kDa.
MMP-3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8147
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

MMP 3 Human, HEK

Matrix Metalloproteinase-3 Human Recombinant, HEK

MMP-3 Human Recombinant produced in HEK293 cells is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa.
MMP-3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8202
Source
HEK293 cells.
Appearance
Sterile Filtered colorless solution.

MMP 7 Human

Matrix Metalloproteinase-7 Human Recombinant

MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.
MMP7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT8275
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

MMP 7 Human, Active

Matrix Metalloproteinase-7 Human Recombinant, Active

Matrix Metalloproteinase-7 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 19.13 kDa.
The MMP-7 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT8353
Source
Escherichia Coli.
Appearance
Sterile clear liquid 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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