|Datasheet||Specific References||Reviews||Related Products||Protocols|
|Vector Type||Mammalian Expression Vector|
|Expression Method||Constiutive ,Stable / Transient|
|Selection In Mammalian Cells||Hygromycin|
A myc tag is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.
A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.
The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.
|Mouse MMP-7 ORF mammalian expression plasmid, C-GFPSpark tag||MG50492-ACG|
|Mouse MMP-7 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50492-ACR|
|Mouse MMP-7 ORF mammalian expression plasmid, C-Flag tag||MG50492-CF|
|Mouse MMP-7 ORF mammalian expression plasmid, C-His tag||MG50492-CH|
|Mouse MMP-7 ORF mammalian expression plasmid, C-Myc tag||MG50492-CM|
|Mouse MMP-7 ORF mammalian expression plasmid, C-HA tag||MG50492-CY|
|Mouse MMP-7 Gene cDNA clone plasmid||MG50492-M|
|Mouse MMP-7 ORF mammalian expression plasmid, N-Flag tag||MG50492-NF|
|Mouse MMP-7 ORF mammalian expression plasmid, N-His tag||MG50492-NH|
|Mouse MMP-7 ORF mammalian expression plasmid, N-Myc tag||MG50492-NM|
|Mouse MMP-7 ORF mammalian expression plasmid, N-HA tag||MG50492-NY|
|Mouse MMP-7 natural ORF mammalian expression plasmid||MG50492-UT|
|Learn more about expression Vectors|
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological and pathological processes such as morphogenesis, differentiation, angiogenesis, tissue remodeling, and tumor invasion. MMPs are synthesized as pro-enzymes and converted to active form by extracellular proteinases. MMP7, also referred to as matrilysin, is the smallest member of the MMP family and differs from other MMP members in that it lacks the C-terminal hemopexin-like domain. MMP7 is produced primarily by mucosal epithelia, and is capable of degrading various ECM proteins including proteoglycans, fibronectin, elastin and casein. This enzyme serves essential functions in both innate defense and wound healing, and appears to be one of the most important MMPs in human colon cancers. It has been reported that MMP7 contributes to tumor malignancy probably by cleaving cell surface proteins such as Fas ligand, degradation of IgG or inducing E-cadherin-mediated cell aggregation. In addition, matrilysin is also identified as a mediator of pulmonary fibrosis and a potential therapeutic target.