MMP-2 Human, HEK

Matrix Metalloproteinase-2 Human Recombinant, HEK
Cat. No.
BT9176
Source
HEK293 cells.
Synonyms
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Appearance
The MMP-2 is supplied as a sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage

THE BioTek'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

MMP-2 Human Recombinant produced in HEK293 cells is a proform of the Human MMP-2 (Ala30-Cys660) and fused with a ployhistide tag at the C-terminus, having an Mw of 71kDa.
MMP-2 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Matrix metalloproteinase-2 (MMP-2), also known as type IV collagenase, plays a crucial role in various physiological processes, including the breakdown of the endometrial lining during menstruation, the formation of new blood vessels (vascularization), and the body's response to injury or infection (inflammatory response). This enzyme possesses several distinct regions, each with a specific function. These regions include a prodomain that is removed for activation, a catalytic domain containing the zinc binding site essential for its enzymatic activity, a fibronectin-like domain thought to be involved in substrate recognition, and a carboxyl-terminal (hemopexin-like) domain with two N-linked glycosylation sites. MMP-2 exhibits broad substrate specificity, capable of degrading various components of the extracellular matrix, including collagens (types IV, V, VII, and X) and gelatin type I. Additionally, it interacts with other molecules like THBS2, TIMP2, Thrombospondin 1, CCL7, and TIMP4, influencing their activities. Interestingly, MMP-2 can undergo autocatalytic cleavage in its C-terminal region, generating a fragment known as PEX, which possesses anti-angiogenic properties. This process appears to be facilitated by the interaction of MMP-2 with integrin β3. Defects in MMP-2 have been linked to a genetic disorder called Torg-Winchester syndrome (TWS), also known as multicentric osteolysis nodulosis and arthropathy (MONA).
Description
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.
Physical Appearance
MMP-2 is provided as a clear, sterile solution that has undergone filtration.
Formulation
MMP-2 is supplied in a 0.2 µm filtered solution containing 20 mM Tris-HCl buffer (pH 7.4), 150 mM NaCl, and 0.05% Brij 35.
Stability
For short-term storage (up to 2-4 weeks), MMP-2 should be kept at 4°C. For extended storage, it is recommended to store the protein frozen at -20°C. To maintain protein integrity, avoid repeated freezing and thawing cycles.
Purity
The purity of MMP-2 is determined to be greater than 95% using SDS-PAGE analysis.
Biological Activity
The enzymatic activity of MMP-2 is assessed based on its ability to cleave a specific fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (available from RND, Catalog # ES001). The specific activity is determined to be greater than 1,000 picomoles per minute per microgram of protein. It's important to note that the recombinant human MMP-2 protein is supplied in its pro-form, which requires activation using p-aminophenylmercuric acetate (APMA) for enzymatic activity. Here's a detailed activation protocol: 1. Dilute the MMP-2 protein to a concentration of 100 µg/ml in the Assay Buffer, which consists of 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij 35, adjusted to pH 7.5. 2. Activate MMP-2 by adding APMA (Sigma, Catalog # A9563) to a final concentration of 1 mM from a 100 mM stock solution prepared in DMSO. 3. Incubate the mixture at 37°C for 1 hour to allow for complete activation.
Synonyms
72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.
Source
HEK293 cells.

Product Science Overview

Introduction

Matrix Metalloproteinase-2 (MMP-2), also known as 72 kDa gelatinase, Gelatinase A, or TBE-1, is a member of the matrix metalloproteinase (MMP) family. MMPs are zinc-dependent endopeptidases involved in the degradation of the extracellular matrix (ECM) components. MMP-2 plays a crucial role in various physiological and pathological processes, including tissue remodeling, embryonic development, reproduction, and disease progression such as arthritis and metastasis .

Structure and Function

MMP-2 is a type IV collagenase that cleaves collagen-like sequences and other ECM components such as fibronectin and elastin. It contains three fibronectin type-II domains and four hemopexin-like domains, which are essential for its substrate specificity and interaction with tissue inhibitors of metalloproteinases (TIMPs) . The enzyme is produced as an inactive pro-protein and becomes activated upon cleavage by extracellular proteinases .

Expression and Production

The human recombinant MMP-2 is expressed in HEK 293 cells, a human embryonic kidney cell line. This expression system allows for human-like glycosylation and proper protein folding, resulting in higher specific activity of the protein . The recombinant MMP-2 is produced as a glycoprotein with a calculated molecular mass of 72 kDa, but it migrates as a 75-80 kDa polypeptide on SDS-PAGE due to glycosylation .

Biological Roles

MMP-2 is involved in various biological processes:

  • Tissue Remodeling: MMP-2 participates in the breakdown and remodeling of the ECM, which is crucial for tissue repair and regeneration .
  • Angiogenesis: It plays a role in the formation of new blood vessels by degrading the ECM components surrounding endothelial cells .
  • Inflammation: MMP-2 is involved in leukocyte migration from the circulation into tissues during inflammation .
  • Disease Processes: MMP-2 is implicated in several pathological conditions, including Chagas’ cardiomyopathy, heart failure, chronic kidney disease, and cancer metastasis .
Therapeutic Potential

Given its involvement in various diseases, MMP-2 is considered a potential therapeutic target. Inhibitors of MMP-2 are being explored for their potential to treat conditions such as cancer, cardiovascular diseases, and inflammatory disorders .

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