MMP 7 Human

Matrix Metalloproteinase-7 Human Recombinant
Cat. No.
BT8275
Source
Escherichia Coli.
Synonyms
Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.
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.
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Description

MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.
MMP7 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Matrix metalloproteinase-7 (MMP-7), alternatively known as matrilysin or PUMP (EC 3.4.24.23), is an enzyme that plays a crucial role in the breakdown of various extracellular matrix components. These include collagen types IV and X, elastin, fibronectin, gelatin, laminin, and proteoglycans. While closely related to the stromelysin family, MMP-7 is encoded by a distinct gene. Structurally, it is the smallest among all MMPs, comprising a pro-peptide domain and a catalytic domain, lacking the hemopexin-like domain found in other MMP members. Initially synthesized as a 28 kDa proenzyme, MMP-7 can be activated in vitro by organomercurials and trypsin, and in vivo by MMP-3, resulting in an 18 kDa active enzyme. Once activated, MMP-7 exhibits the capacity to activate pro-MMP-1 and pro-MMP-9, but not pro-MMP-2. Notably, MMP-7 demonstrates widespread expression, with elevated levels observed in cycling endometrium, colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately half of all gliomas.
Description
Recombinant human MMP-7, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 174 amino acids (residues 95-267). It has a molecular weight of 19.2 kDa. The purification of MMP-7 is achieved through proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
MMP-7 is provided as a protein solution at a concentration of 1 mg/ml. The solution is buffered with 20 mM Tris at pH 8.0 and contains 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the MMP-7 solution can be stored at 4°C. For longer storage, it is recommended to store the solution frozen at -20°C. To ensure stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advised. It's important to avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of MMP-7 is determined to be greater than 90% based on SDS-PAGE analysis.
Synonyms
Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.
Source
Escherichia Coli.
Amino Acid Sequence
MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK.

Product Science Overview

Introduction

Matrix Metalloproteinase-7 (MMP-7), also known as matrilysin, is a member of the matrix metalloproteinase (MMP) family. This family consists of structurally related zinc-dependent endopeptidases that play a crucial role in the breakdown of extracellular matrix (ECM) components. MMP-7 is the smallest member of the MMP family and is encoded by the MMP7 gene located on human chromosome 11q21-q22 .

Discovery and Structure

MMP-7 was first discovered by Sellers and Woessner in the uterus of the rat in 1988 . The complementary DNA (cDNA) of human MMP7 was isolated in the same year by Muller et al . Human MMP-7 has a molecular weight of approximately 30 kDa . Unlike other MMPs, MMP-7 lacks a conserved C-terminal hemopexin-like domain, which is typically involved in substrate specificity and interaction with tissue inhibitors of metalloproteinases (TIMPs) .

Biological Functions

MMP-7 is primarily involved in the degradation of ECM components, including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan . This enzyme is exclusively released by epithelial cells and is highly expressed in various cancer cells . MMP-7 plays a significant role in normal physiological processes such as embryonic development, reproduction, and tissue remodeling. Additionally, it is implicated in pathological processes like arthritis and metastasis .

Clinical Significance

Elevated expression of MMP-7 has been associated with the progression and metastasis of various cancers, including tongue squamous cell carcinoma (TSCC) . Studies have shown that high levels of MMP-7 promote cell proliferation, migration, and invasion in cancer cells . As a result, MMP-7 is considered a potential therapeutic target for cancer treatment.

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MMP 7 Human, Active
Matrix Metalloproteinase-7 Human Recombinant, Active
Cat. No.
BT8353
Source
Escherichia Coli.
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