MT1-MMP [MMP-14]

Key Applications	Entrez Gene Number	Species	Uni Prot Number
FUNC	NM_004995.2	Human	P50281

Key Applications

Entrez Gene Number

Species

Uni Prot Number

FUNC

NM_004995.2

Human

P50281

Description
Catalogue Number	CC1043
Brand Family	Chemicon®
Trade Name	Chemicon
Description	MMP-14, human, prodomain, catalytic domain, and hemopexin domain, E. coli recombinant
Overview	CC1043 is a recombinant polypeptide sequence produced as a periplasmic protein in E. coli. The proenzyme consists of MT1-MMP residues corresponding to Ser1-Val501 followed by tone Thr-residue and six His-residues. The calculated Mr of the recombinant soluble proenzyme is 58200 Da.
Alternate Names	MT1-MMP
Background Information	BACKGROUND: Matrix metalloproteinases (MMPs) are Zn2+- and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components [Matrisian, 1992]. Presently, eighteen secreted MMPs and five membrane-type MMPs [Sato et al., 1994; Will & Hinzmann, 1995; Takino et al., 1995; Puente et al., 1996] are known to be expressed in vertebrates. Human MT1-MMP consists of 559 amino acid residues with a calculated Mr of 63516 [Sato et al., 1994; Will & Hinzmann, 1995]. The following domains and sequence regions are distinguished in MT1-MMP: Prodomain (Ser1-Arg88), catalytic domain (Tyr89-Gly261), junction between catalytic domain and hemopexin domain (Gly262-Gly292), hemopexin-like domain (Pro293-Cys485) and C-terminal sequence (Pro486-Val559) with transmembrane segment. A soluble form of MT1-MMP without transmembrane segment has been found in culture medium of a breast carcinoma cell line [Imai et al., 1996]. MT1-MMP is expressed in adult lung, placenta, kidney, ovaries, intestine, prostate and spleen [Will & Hinzmann, 1995]. Increased amounts of the enzyme are found in tumor tissues such as lung carcinoma [Butler et al., 1998], gastric carcinoma [Nomura et al., 1995], breast, head and neck carcinoma [Okada et al., 1995]. MT1-MMP is activated by removal of its prodomain. The reaction is catalyzed by furin, a subtilysin-type serine protease, which recognizes a motif of four basic amino acid residues located between the prodomain and catalytic domain [Pei & Weiss, 1996]. MT1-MMP activates progelatinase A [Sato et al., Strongin et al., 1995; Will et al., 1996] and procollagenase-3 [Knauper et al., 1996] by proteolytic cleavage of their domains. The ability of MT1-MMP to activate other matrix metalloproteinases provides potential for enhanced pericellular proteolysis in physiological and pathological processes. In particular, activation of progelatinase A by MT1-MMP is considered to contribute to local degradation of extracellular matrix during cell migration and proliferation. MT1-MMP also hydrolyzes fibrillar collagens I, II and III into characteristic ¾ and ¼ fragments [D'Ortho et al., 1997; Ohuci et al., 1997] and it cleaves a number of other ECM proteins, including fibronectin, vitronectin, laminin-1 and dermatan sulfate proteoglycan [D'Ortho et al., 1997; Pei & Weiss, 1996; Ohuci et al., 1997]. The activity of MT1-MMP is poorly inhibited by TIMP-1 but efficiently inhibited by TIMP-2 and TIMP-3 [Will et al., 1996].

Description

Catalogue Number

CC1043

Brand Family

Chemicon®

Trade Name

Chemicon

Description

MMP-14, human, prodomain, catalytic domain, and hemopexin domain, E. coli recombinant

Overview

CC1043 is a recombinant polypeptide sequence produced as a periplasmic protein in E. coli. The proenzyme consists of MT1-MMP residues corresponding to Ser1-Val501 followed by tone Thr-residue and six His-residues. The calculated Mr of the recombinant soluble proenzyme is 58200 Da.

Alternate Names

MT1-MMP

Background Information

BACKGROUND: Matrix metalloproteinases (MMPs) are Zn2+- and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components [Matrisian, 1992]. Presently, eighteen secreted MMPs and five membrane-type MMPs [Sato et al., 1994; Will & Hinzmann, 1995; Takino et al., 1995; Puente et al., 1996] are known to be expressed in vertebrates. Human MT1-MMP consists of 559 amino acid residues with a calculated Mr of 63516 [Sato et al., 1994; Will & Hinzmann, 1995]. The following domains and sequence regions are distinguished in MT1-MMP: Prodomain (Ser1-Arg88), catalytic domain (Tyr89-Gly261), junction between catalytic domain and hemopexin domain (Gly262-Gly292), hemopexin-like domain (Pro293-Cys485) and C-terminal sequence (Pro486-Val559) with transmembrane segment. A soluble form of MT1-MMP without transmembrane segment has been found in culture medium of a breast carcinoma cell line [Imai et al., 1996].

MT1-MMP is expressed in adult lung, placenta, kidney, ovaries, intestine, prostate and spleen [Will & Hinzmann, 1995]. Increased amounts of the enzyme are found in tumor tissues such as lung carcinoma [Butler et al., 1998], gastric carcinoma [Nomura et al., 1995], breast, head and neck carcinoma [Okada et al., 1995].

MT1-MMP is activated by removal of its prodomain. The reaction is catalyzed by furin, a subtilysin-type serine protease, which recognizes a motif of four basic amino acid residues located between the prodomain and catalytic domain [Pei & Weiss, 1996].

MT1-MMP activates progelatinase A [Sato et al., Strongin et al., 1995; Will et al., 1996] and procollagenase-3 [Knauper et al., 1996] by proteolytic cleavage of their domains. The ability of MT1-MMP to activate other matrix metalloproteinases provides potential for enhanced pericellular proteolysis in physiological and pathological processes. In particular, activation of progelatinase A by MT1-MMP is considered to contribute to local degradation of extracellular matrix during cell migration and proliferation. MT1-MMP also hydrolyzes fibrillar collagens I, II and III into characteristic ¾ and ¼ fragments [D'Ortho et al., 1997; Ohuci et al., 1997] and it cleaves a number of other ECM proteins, including fibronectin, vitronectin, laminin-1 and dermatan sulfate proteoglycan [D'Ortho et al., 1997; Pei & Weiss, 1996; Ohuci et al., 1997]. The activity of MT1-MMP is poorly inhibited by TIMP-1 but efficiently inhibited by TIMP-2 and TIMP-3 [Will et al., 1996].

Product Information
Presentation	Provided as a liquid in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl2.

Product Information

Presentation

Provided as a liquid in 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl2.

Applications
Key Applications	Affects Function
Application Notes	Useful as an antigen standard in immunoassays. The proenzyme can be activated with trace amounts of MT1-MMP catalytic domain (D'Ortho et al., 1997; Butler et al., 1998).

Applications

Key Applications

Affects Function

Application Notes

Useful as an antigen standard in immunoassays. The proenzyme can be activated with trace amounts of MT1-MMP catalytic domain (D'Ortho et al., 1997; Butler et al., 1998).

Biological Information
Concentration	5 μg/25μL
Purity	Appears as a predominant band at 58 kDa in SDS-PAGE
Entrez Gene Number	NM_004995.2
Entrez Gene Summary	Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.
Gene Symbol	MMP14 MTMMP1 MMP-14 MT1MMP MT1-MMP MMP-X1 EC 3.4.24.80
UniProt Number	P50281
UniProt Summary	FUNCTION: SwissProt: P50281 # Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. COFACTOR: Binds 1 zinc ion per subunit (By similarity). & Calcium (By similarity). SIZE: 582 amino acids; 65884 Da SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (Potential). Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. TISSUE SPECIFICITY: In stromal cells of colon, breast, and head and neck. DOMAIN: SwissProt: P50281 The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. SIMILARITY: Belongs to the peptidase M10A family. & Contains 4 hemopexin-like domains.

Biological Information

Concentration

5 μg/25μL

Purity

Appears as a predominant band at 58 kDa in SDS-PAGE

Entrez Gene Number

NM_004995.2

Entrez Gene Summary

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion.

Gene Symbol

MMP14
MTMMP1
MMP-14
MT1MMP
MT1-MMP
MMP-X1
EC 3.4.24.80

UniProt Number

P50281

UniProt Summary

FUNCTION: SwissProt: P50281 # Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface.
COFACTOR: Binds 1 zinc ion per subunit (By similarity). & Calcium (By similarity).
SIZE: 582 amino acids; 65884 Da
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (Potential). Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
TISSUE SPECIFICITY: In stromal cells of colon, breast, and head and neck.
DOMAIN: SwissProt: P50281 The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
SIMILARITY: Belongs to the peptidase M10A family. & Contains 4 hemopexin-like domains.

Product Usage Statements
Usage Statement	Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Product Usage Statements

Usage Statement

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage and Shipping Information
Storage Conditions	Maintain frozen at -70°C in undiluted aliquots. The enzyme may be stored at -20°C for several weeks. Repeated freezing and thawing should be avoided

Storage and Shipping Information

Storage Conditions

Maintain frozen at -70°C in undiluted aliquots. The enzyme may be stored at -20°C for several weeks. Repeated freezing and thawing should be avoided

Packaging Information
Material Size	5 µg

Packaging Information

Material Size

5 µg

实验耗材

分子生物学试剂

蛋白与免疫学

生化试剂

细胞及检测试剂

色谱及层析

仪器设备

实验服务

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