Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain Recombinant Protein
Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain (MT1-MMP, MMP-14, Collagenase-3) Recombinant
Applications
ELISA
Purity
PurifiedAppears as a predominant band at 58kD in SDS-PAGE (> 80% total protein)
Synonyms
Matrix Metalloproteinase 14; Pro Domain-catalytic Domain-hemopexin Domain; Pro Domain-catalytic Domain-hemopexin Domain (MT1-MMP; MMP-14; Collagenase-3) Recombinant; Pro Domain-catalytic Domain-hemopexin Domain recombinant protein
Host
Human recombinant from E Coli
Purity/Purification
Purified
Appears as a predominant band at 58kD in SDS-PAGE (> 80% total protein)
Appears as a predominant band at 58kD in SDS-PAGE (> 80% total protein)
Form/Format
Provided as a liquid in 50mM Tris-HCl, pH 7.5, 150mM sodium chloride, 5mM CaCl2.
Applicable Applications for Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain recombinant protein
ELISA (EL/EIA)
Application Notes
Useful as an antigen standard in immunoassays. The proenzyme can be activated with trace amounts of MT1-MMP catalytic domain (1,2).
Preparation and Storage
-20 degree C
Related Product Information for Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain recombinant protein
Matrix metalloproteinases (MMPs) are Zn2+-and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components (1). Presently, eighteen secreted MMPs and five membrane-type MMPs (2-5) are known to be expressed in vertebrates. Human MT1-MMP consists of 559 amino acid residues with a calculated Mr of 63516 (2,3). 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. When expressed in cells, the catalytic domain and the hemopexin domain of MT1-MMP become exposed on cell surfaces (2,6). A soluble form of MT1-MMP without transmembrane segment has been found in culture medium of a breast carcinoma cell line (7). MT1-MMP is expressed in adult lung, placenta, kidney, ovaries, intesting, prostate and spleen (3). Increased amounts of the enzyme are found in tumor tissues such as lung carcinoma (2), gastric carcinoma (8), breast, head and neck carcinoma (9). 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 (6). MT1-MMP activates progelatinase A (2,10,11) and procollagenase-3 (12) 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 3/4 and 1/4 fragments (13) and it cleaves a number of other ECM proteins, including fibronectin, vitronectin, laminin-1 and dermatan sulfate proteoglycan (6,13). The activity of MT1-MMP is poorly inhibited by TIMP-1 but efficiently inhibited by TIMP-2 and TIMP-3 (11). The recombinant prodomain and catalytic domain of MT1-MMP is useful for the study of Progelatinase A (MMP-2) activation and the degradation of proteins of the extracellular matrix. The enzyme allows screening of matrix metalloproteinase inhibitors and characterization of inhibitor action.
Recombinant polypeptide sequence produced as a periplasmic protein in E. coli. The pro-MT1-MMP deletion mutant consists of MT1-MMP residues corresponding to Ser1-Gly265 followed by the His-tag sequence Leu-Val-Thr-(His)6. The calculated Mr of the recombinant proenzyme is 30860 Da. Upon activation with trypsin the prodomain sequence Ser1-Arg88 is removed from recombinant pro-MT1MMP and enzymatically active catalytic domain beginning with Tyr89 is liberated.
Recombinant polypeptide sequence produced as a periplasmic protein in E. coli. The pro-MT1-MMP deletion mutant consists of MT1-MMP residues corresponding to Ser1-Gly265 followed by the His-tag sequence Leu-Val-Thr-(His)6. The calculated Mr of the recombinant proenzyme is 30860 Da. Upon activation with trypsin the prodomain sequence Ser1-Arg88 is removed from recombinant pro-MT1MMP and enzymatically active catalytic domain beginning with Tyr89 is liberated.
Product Categories/Family for Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain recombinant protein
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Product Notes
The Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain (Catalog #AAA635999) is a Recombinant Protein produced from Human recombinant from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain can be used in a range of immunoassay formats including, but not limited to, ELISA (EL/EIA). Useful as an antigen standard in immunoassays. The proenzyme can be activated with trace amounts of MT1-MMP catalytic domain (1,2). Researchers should empirically determine the suitability of the Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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