ProMMP 9 Human
Pro-Matrix Metalloproteinase-9 Human Recombinant
Cat. No.
BT9894
Source
Escherichia Coli.
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
Pro-MMP-9 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 688 amino acids fragment (20-707) corresponding to the pro form of the protein minus the signal peptide, having a total molecular mass of 78.59kDa and fused with a 4.5kDa amino-terminal hexahistidine tag.
The Pro-MMP-9 is purified by proprietary chromatographic techniques.
The Pro-MMP-9 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Matrix metalloproteinases (MMPs) are a family of enzymes that depend on zinc and calcium to break down proteins found in the extracellular matrix. MMP9, initially produced as a 92kDa inactive precursor (zymogen), undergoes cleavage to become active, resulting in an 82kDa enzyme. Structurally, MMP9 consists of several domains: a gelatin-binding domain with three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain, and a hemopexin-like domain. Various cells, including monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, and endothelial cells, produce MMP9. This enzyme plays a crucial role in inflammatory responses, tissue remodeling, wound healing, tumor growth, and metastasis. Additionally, MMP9 contributes to the breakdown of the extracellular matrix, facilitates leukocyte migration, and participates in bone resorption by osteoclasts. MMP9 acts on type IV and type V collagens, breaking them down into larger C-terminal three-quarter fragments and smaller N-terminal one-quarter fragments. Furthermore, MMP9 can degrade fibronectin but not laminin or Pz-peptide. Defects in MMP9 have been linked to an increased susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).
Description
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.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
Pro-MMP-9 protein is supplied in a buffer solution of 1x PBS (phosphate-buffered saline) with 50% glycerol.
Stability
For short-term storage (up to 4 weeks), the entire vial should be kept at 4°C. For longer storage, it should be frozen at -20°C. Avoid repeated freezing and thawing cycles.
Purity
The purity of Pro-MMP-9 is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Source
Escherichia Coli.
Product Science Overview
Structure and Activation
Biological Functions
MMP-9 is produced by various cell types, including monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, and endothelial cells . It is involved in several physiological and pathological processes:
- Inflammatory responses: MMP-9 is upregulated during inflammation and contributes to the remodeling of the ECM.
- Tissue remodeling: It plays a role in wound healing by degrading ECM components to allow cell migration and tissue repair.
- Tumor growth and metastasis: MMP-9 facilitates tumor invasion and metastasis by breaking down ECM barriers.
- Bone remodeling: It is involved in the resorption of bone matrix by osteoclasts .
Recombinant Human MMP-9
Recombinant human MMP-9 is produced using various expression systems, including Chinese Hamster Ovary (CHO) cells and E. coli . The recombinant protein is often used in research to study its structure, function, and role in various diseases. It is supplied in different formulations, with or without carrier proteins like Bovine Serum Albumin (BSA), depending on the intended application .
Applications
Recombinant MMP-9 is widely used in:
- Biochemical assays: To study its enzymatic activity and substrate specificity.
- Cell culture: To investigate its effects on cell behavior and ECM remodeling.
- Drug development: As a target for inhibitors aimed at treating diseases associated with excessive ECM degradation, such as cancer and fibrosis .
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