MMP1 Human, sf9

Matrix Metalloproteinase-1 Human Recombinant, sf9
Cat. No.
BT8799
Source
Sf9, Baculovirus cells.
Synonyms
Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% 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

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.

Product Specs

Introduction
MMP-1, also known as interstitial collagenase, is an enzyme that plays a crucial role in the breakdown of various substrates within the extracellular matrix. These substrates include collagen types I, II, III, VII, VIII, and X, as well as other molecules like L-Selectin, pro-TNF, IL-1β, IGFBP-3, IGFBP-5, casein, gelatin, α1-antitrypsin, myelin basic protein, pro-MMP2, and pro-MMP9. Notably, MMP-1 is essential for the degradation of fibrillar collagens, contributing significantly to the remodeling of the extracellular matrix. The enzyme is produced by various cell types, including fibroblasts, keratinocytes, endothelial cells, monocytes, and macrophages. Structurally, MMP-1 comprises several distinct domains: a prodomain that gets cleaved upon activation, a catalytic domain harboring the zinc binding site, a short hinge region, and a carboxyl-terminal domain. Genetically, MMP-1 is part of a cluster of MMP genes located on chromosome 11q22.3.
Description
Recombinant Human MMP1, expressed in Sf9 Baculovirus cells, is a non-glycosylated polypeptide chain. This single chain protein consists of 460 amino acids (18-469), with a molecular weight of 53.1 kDa. It's important to note that on SDS-PAGE, the apparent molecular size might appear between 50-70 kDa. This MMP1 protein has an 8 amino acid His-tag fused at its C-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The MMP1 protein solution is provided at a concentration of 0.25 mg/ml. The solution is buffered with 20mM MES buffer (pH 5.5) and contains 10mM CaCl2, 100 mM NaCl, 0.05% Brij35, and 30% glycerol.
Stability
For short-term storage (up to 4 weeks), the MMP1 protein solution can be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To ensure stability during long-term storage, it is advisable to add a carrier protein such as HSA or BSA (0.1%). It is important to avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the MMP1 protein is greater than 95% as determined by SDS-PAGE analysis.
Synonyms
Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
HSFPATLETQ EQDVDLVQKY LEKYYNLKND GRQVEKRRNS GPVVEKLKQM QEFFGLKVTG KPDAETLKVM KQPRCGVPDV AQFVLTEGNP RWEQTHLTYR IENYTPDLPR ADVDHAIEKA FQLWSNVTPL TFTKVSEGQA DIMISFVRGD HRDNSPFDGP GGNLAHAFQP GPGIGGDAHF DEDERWTNNF REYNLHRVAA HELGHSLGLS HSTDIGALMY PSYTFSGDVQ LAQDDIDGIQ AIYGRSQNPV QPIGPQTPKA CDSKLTFDAI TTIRGEVMFF KDRFYMRTNP FYPEVELNFI SVFWPQLPNG LEAAYEFADR DEVRFFKGNK YWAVQGQNVL HGYPKDIYSS FGFPRTVKHI DAALSEENTG KTYFFVANKY WRYDEYKRSM DPGYPKMIAH DFPGIGHKVD AVFMKDGFFY FFHGTRQYKF DPKTKRILTL QKANSWFNCR KNLEHHHHHH.

Product Science Overview

Introduction

Matrix Metalloproteinase-1 (MMP-1), also known as interstitial collagenase, is a member of the matrix metalloproteinase (MMP) family. These enzymes are responsible for the degradation of extracellular matrix components, playing a crucial role in tissue remodeling, wound healing, and various pathological processes such as arthritis and cancer metastasis. MMP-1 specifically targets interstitial collagens, including types I, II, and III, breaking down their triple-helical structure.

Human Recombinant MMP-1

Human recombinant MMP-1 is produced using recombinant DNA technology, which involves inserting the human MMP-1 gene into a host cell to produce the enzyme. The recombinant form of MMP-1 is often used in research to study its structure, function, and role in various biological processes. The recombinant enzyme is typically expressed in different host systems, including bacterial, yeast, and insect cells.

Expression in Sf9 Cells

Sf9 cells, derived from the fall armyworm (Spodoptera frugiperda), are commonly used in the baculovirus expression system for producing recombinant proteins. This system is advantageous due to its high expression levels, proper protein folding, and post-translational modifications. Human recombinant MMP-1 produced in Sf9 cells is a non-glycosylated polypeptide chain containing 460 amino acids, with a molecular mass of approximately 53.1 kDa .

Preparation Methods

The preparation of human recombinant MMP-1 in Sf9 cells involves several steps:

  1. Gene Cloning: The human MMP-1 gene is cloned into a baculovirus transfer vector.
  2. Transfection: Sf9 cells are transfected with the recombinant baculovirus vector.
  3. Protein Expression: The transfected Sf9 cells produce the recombinant MMP-1 protein.
  4. Purification: The recombinant protein is purified using chromatographic techniques to achieve high purity and activity.
Chemical Reactions and Analysis

MMP-1 initiates the breakdown of interstitial collagens by cleaving the triple-helical structure of these collagens. The enzyme’s activity is often measured using fluorogenic peptide substrates, which release a fluorescent signal upon cleavage by MMP-1. This allows researchers to quantify the enzyme’s activity and study its kinetics.

The biological activity of recombinant MMP-1 is crucial for understanding its role in physiological and pathological processes. For instance, MMP-1’s ability to degrade collagen is essential for tissue remodeling but can also contribute to disease progression in conditions like arthritis and cancer.

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 1 Human
Matrix Metalloproteinase-1 Human Recombinant
Cat. No.
BT7829
Source
Escherichia Coli.
MMP 1 Human, HEK
Matrix Metalloproteinase-1 Human Recombinant, HEK
Cat. No.
BT7919
Source
HEK293 cells.
MMP1 (24-207) Human
Matrix Metalloproteinase-1 (24-207 a.a) Human Recombinant, HEK
Cat. No.
BT8721
Source
<p><span lang="EN-US">HEK293 Cells.</span></p>
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.