|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 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 CTSB ORF mammalian expression plasmid, C-GFPSpark tag||MG50084-ACG|
|Mouse CTSB ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50084-ACR|
|Mouse CTSB ORF mammalian expression plasmid, C-Flag tag||MG50084-CF|
|Mouse CTSB ORF mammalian expression plasmid, C-His tag||MG50084-CH|
|Mouse CTSB ORF mammalian expression plasmid, C-Myc tag||MG50084-CM|
|Mouse CTSB ORF mammalian expression plasmid, C-HA tag||MG50084-CY|
|Mouse CTSB Gene cDNA clone plasmid||MG50084-M|
|Mouse CTSB ORF mammalian expression plasmid, N-Flag tag||MG50084-NF|
|Mouse CTSB ORF mammalian expression plasmid, N-His tag||MG50084-NH|
|Mouse CTSB ORF mammalian expression plasmid, N-Myc tag||MG50084-NM|
|Mouse CTSB ORF mammalian expression plasmid, N-HA tag||MG50084-NY|
|Mouse CTSB natural ORF mammalian expression plasmid||MG50084-UT|
|Learn more about expression Vectors|
Cathepsin B is a papain-family cysteine protease that is normally located in lysosomes, where it is involved in the turnover of proteins and plays various roles in maintaining the normal metabolism of cells. This protease has been implicated in pathological conditions, e.g., tumor progression and arthritis. In disease conditions, increases in the expression of cathepsin B occur at both the gene and protein levels. Cathepsin B is synthesized as a preproenzyme and the primary pathways for its normal trafficking to the lysosome utilize mannose 6-phosphate receptors (MPRs). Mature cathepsin B has the ability to degrade several extracellular matrix components at both neutral and acidic pH and has been implicated in the progression of several human and rodent tumors progression and arthritis. Cathepsin B expression is increased in many human cancers at the mRNA, protein and activity levels. It is also frequently overexpressed in premalignant lesions, an observation that associates this protease with local invasive stages of cancer. Increased expression of cathepsin B in primary cancers, and especially in preneoplastic lesions, suggests that this enzyme might have pro-apoptotic features. Active cathepsin B is also secreted from tumours, a mechanism likely to be facilitated by lysosomal exocytosis or extracellular processing by surface activators. Cathepsin B is localized to caveolae on the tumour surface, where binding to the annexin II heterotetramer occurs. Thus CTSB is suggested as a tumor marker. Additionally, Cathepsin B can degrade extracellular matrix proteins, such as collagen IV and laminin, and can activate the precursor form of urokinase plasminogen activator (uPA), perhaps thereby initiating an extracellular proteolytic cascade.