MMP 3 Human

Matrix Metalloproteinase-3 Human Recombinant
Cat. No.
BT8069
Source
Escherichia Coli.
Synonyms
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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.
Shipped with Ice Packs
In Stock
Quick Inquiry

Description

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.

Product Specs

Introduction
MMP-3, also known as Stromelysin-1 or Transin-1, is an enzyme that breaks down natural collagen at normal body pH and temperature. It plays a role in the degradation of the intervertebral disc, particularly in cases of herniated lumbar discs. MMP-3 targets various components of the extracellular matrix, including proteoglycan, laminin, fibronectin, gelatin, and collagen types III, IV, and IX. Additionally, it activates pro-MMP-9 and pro-MMP-8, and enhances the activity of plasmin-activated MMP-1. Initially produced in an inactive form (proenzyme), MMP-3 is activated by enzymes like plasmin, trypsin, chymotrypsin, cathepsin G, and human neutrophil elastase. Notably, MMP-3 has been shown to activate the precursor of IL1-beta.
Description
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.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The MMP-3 solution is provided at a concentration of 0.25 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store the vial at 4°C. For longer storage, freeze the solution at -20°C. Adding a carrier protein such as HSA or BSA (0.1%) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the MMP-3 protein is greater than 90% as assessed by SDS-PAGE.
Synonyms
CHDS6, MMP-3, SL-1, STMY, STMY1, STR1, Stromelysin-1, Matrix metalloproteinase-3, Transin-1, MMP3.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFRTFPGI PKWRKTHLTY RIVNYTPDLP KDAVDSAVEK ALKVWEEVTP LTFSRLYEGE ADIMISFAVR EHGDFYPFDG PGNVLAHAYA PGPGINGDAH FDDDEQWTKD TTGTNLFLVA AHEIGHSLGL FHSANTEALM YPLYHSLTDL TRFRLSQDDI NGIQSLYGPP PDSPETPLVP TEPVPPEPGT PANCDPALSF DAVSTLRGEI LIFKDRHFWR KSLRKLEPEL HLISSFWPSL PSGVDAAYEV TSKDLVFIFK GNQFWAIRGN EVRAGYPRGI HTLGFPPTVR KIDAAISDKE KNKTYFFVED KYWRFDEKRN SMEPGFPKQI AEDFPGIDSK IDAVFEEFGF FYFFTGSSQL EFDPNAKKVT HTLKSNSWLN C.

Product Science Overview

Introduction

Matrix Metalloproteinase-3 (MMP-3), also known as stromelysin-1, is a member of the matrix metalloproteinase (MMP) family. This family of enzymes is crucial for the degradation of extracellular matrix (ECM) components, which is essential for various physiological processes such as tissue remodeling, wound healing, and embryogenesis .

Structure and Composition

MMP-3 is composed of 475–478 amino acids in mammals, and its amino acid sequence is highly conserved among different species and genera . The structure of MMP-3 can be divided into four parts:

  1. Propeptide: Approximately 80 amino acids.
  2. Metalloproteinase Catalytic Domain: Approximately 170 amino acids.
  3. Hinged Region: A ligating peptide of variable length.
  4. Heme Protein Domain: Approximately 200 amino acids .
Function and Mechanism

MMP-3 is capable of degrading a variety of ECM components, including collagen, gelatin, fibronectin, and laminin . It can also activate multiple pro-MMPs, initiating the MMP-mediated degradation reactions . This enzyme plays a significant role in cellular fibrinolytic activity and is involved in the processing of various pro-MMPs .

Biological Properties

MMP-3 is an exocrine protein that is usually secreted through exocytosis and extracellular vesicles (EVs) . It binds to zinc and calcium ions, which are essential for its metallo-endopeptidase activity . The enzyme is secreted in its pro-protein form and is activated by extracellular proteinase cleavage .

Role in Disease and Cell Differentiation

MMP-3 has been implicated in the pathogenesis of various diseases, including osteoarthritis . It plays both promoting and destabilizing roles in disease progression and cell differentiation . The enzyme’s activity is regulated by various pathways, and its imbalance can lead to significant consequences for diseases such as cancer, cardiovascular disease, and chronic leg ulcers .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *

Category

Service

Related Products

MMP 3 Human, GST
Matrix Metalloproteinase-3 Human Recombinant, GST Tag
Cat. No.
BT8147
Source
Escherichia Coli.
MMP 3 Human, HEK
Matrix Metalloproteinase-3 Human Recombinant, HEK
Cat. No.
BT8202
Source
HEK293 cells.
THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
  • Contact
  • Address: 1925 E Maple Ave, El Segundo, CA 90245 United States
  • Phone : +1 201-285-7826
  • Email : info@thebiotek.com
  • Hours : Mon.-Fri. 9:00 AM - 5:00 PM
© Copyright 2024 Thebiotek. All Rights Reserved.