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pMD18-T Simple Vector is a high-efficiency TA cloning vector constructed from pUC18, of which the initial multiple cloning sites (MCS) were destroyed. Thus the cDNA should be amplified by PCR with primers containing a restriction site for subclone. Competent cells appropriate for pUC18 are also appropriated for the Vector, e.g. JM109, DH5α, TOP10. The pMD18-T Simple Vector is 2.6kb in size. Selection of the plasmid in E. coli is conferred by the ampicillin resistance gene. The coding sequence was inserted by TA cloning at site 425.
The coding sequence can be amplified by PCR with M13-47 and RV-M primers.
|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 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|
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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.