MMP 1 Human

Matrix Metalloproteinase-1 Human Recombinant
Cat. No.
BT7829
Source
Escherichia Coli.
Synonyms

CLG, CLGN, Matrix metalloproteinase-1, MMP-1.

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

Description

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.

Product Specs

Introduction
Matrix metalloproteinase-1 (MMP-1), also known as interstitial collagenase and fibroblast collagenase, is a secreted protein that degrades a variety of substrates, including collagen types I, II, III, VII, VIII, and X, as well as L-selectin, pro-TNF, IL-1β, IGFBP-3, IGFBP-5, casein, gelatin, α1 antitrypsin, myelin basic protein, pro-MMP2, and pro-MMP9. A key function of MMP-1 is the breakdown of fibrillar collagens during extracellular matrix remodeling. This enzyme is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes, and macrophages. Structurally, MMP-1 comprises several distinct domains: a prodomain that is cleaved upon activation, a catalytic domain harboring the zinc binding site, a short hinge region, and a carboxyl terminal domain. The gene encoding MMP-1 is part of a cluster of MMP genes located on chromosome 11q22.3.
Description
Recombinant human MMP-1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 393 amino acids (residues 100-469), including a 23-amino acid N-terminal His-tag, and has a molecular weight of 45 kDa.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
MMP-1 is supplied as a 1 mg/ml solution in 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M urea.
Stability
For short-term storage (2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms

CLG, CLGN, Matrix metalloproteinase-1, MMP-1.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFVLTEGN PRWEQTHLTY RIENYTPDLP RADVDHAIEK AFQLWSNVTP LTFTKVSEGQ ADIMISFVRG DHRDNSPFDG PGGNLAHAFQ PGPGIGGDAH FDEDERWTNN FREYNLHRVA AHELGHSLGL SHSTDIGALM YPSYTFSGDV QLAQDDIDGI QAIYGRSQNP VQPIGPQTPK ACDSKLTFDA ITTIRGEVMF FKDRFYMRTN PFYPEVELNF ISVFWPQLPN GLEAAYEFAD RDEVRFFKGN KYWAVQGQNV LHGYPKDIYS SFGFPRTVKH IDAALSEENT GKTYFFVANK YWRYDEYKRS MDPGYPKMIA HDFPGIGHKV DAVFMKDGFF YFFHGTRQYK FDPKTKRILT LQKANSWFNC RKN.

Product Science Overview

Introduction

Matrix Metalloproteinase-1 (MMP-1), also known as interstitial collagenase or collagenase-1, is a member of the matrix metalloproteinase (MMP) family. These enzymes are crucial for the degradation of extracellular matrix (ECM) components, playing significant roles in both physiological and pathological processes. MMP-1 is particularly known for its ability to degrade fibrillar collagens, which are major structural components of the ECM .

Structure and Activation

MMP-1, like other MMPs, is synthesized as an inactive zymogen. It contains a pro-peptide domain that must be cleaved to activate the enzyme. The pro-peptide domain includes a conserved cysteine residue that interacts with the zinc ion in the active site, keeping the enzyme inactive. Upon activation, the pro-peptide is removed, allowing the enzyme to cleave its substrates .

The active form of MMP-1 consists of three main domains:

  1. Pro-peptide domain: This domain is responsible for maintaining the enzyme in its inactive form.
  2. Catalytic domain: This domain contains the active site, including a zinc ion essential for the enzyme’s catalytic activity.
  3. Haemopexin-like C-terminal domain: This domain is involved in substrate recognition and binding .
Biological Functions

MMP-1 plays a pivotal role in the remodeling of the extracellular matrix. It is capable of degrading type I, II, and III collagens, which are the most abundant collagens in the human body. This degradation is essential for various physiological processes, including tissue repair, embryonic development, and angiogenesis .

In addition to its physiological roles, MMP-1 is also involved in pathological conditions. Overexpression of MMP-1 has been linked to various diseases, such as arthritis, cancer, and cardiovascular diseases. In these conditions, excessive degradation of the ECM can lead to tissue damage and disease progression .

Recombinant MMP-1

Recombinant MMP-1 is produced using genetic engineering techniques, where the human MMP-1 gene is inserted into a suitable expression system, such as bacteria or mammalian cells. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. Recombinant MMP-1 is often used in studies to understand its structure, function, and role in various diseases .

Applications
  1. Research: Recombinant MMP-1 is widely used in research to study its enzymatic activity, substrate specificity, and inhibition. It is also used to investigate the role of MMP-1 in various physiological and pathological processes.
  2. Therapeutics: Understanding the role of MMP-1 in diseases has led to the development of MMP inhibitors as potential therapeutic agents. These inhibitors aim to reduce the excessive ECM degradation observed in conditions like cancer and arthritis .

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