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The pGEM-T is 3kb in length, and contains the amplicin resistance gene, conferring selection of the plasmid in E. coli, and the ori site which is the bacterial origin of replication. The plasmid has multiple cloning sites as shown below. The coding sequence was inserted by TA cloning. Many E. coli strains are suitable for the propagation of this vector including JM109, DH5α and TOP10.
The coding sequence can be easily obtained by digesting the vector with proper restriction enzyme(s). The coding sequence can also be amplified by PCR with M13 primers, or primer pair SP6 and T7.
|Mouse FAP ORF mammalian expression plasmid, C-GFPSpark tag||MG50996-ACG|
|Mouse FAP ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50996-ACR|
|Mouse FAP ORF mammalian expression plasmid, C-Flag tag||MG50996-CF|
|Mouse FAP ORF mammalian expression plasmid, C-His tag||MG50996-CH|
|Mouse FAP ORF mammalian expression plasmid, C-Myc tag||MG50996-CM|
|Mouse FAP ORF mammalian expression plasmid, C-HA tag||MG50996-CY|
|Mouse FAP ORF mammalian expression plasmid, N-Flag tag||MG50996-NF|
|Mouse FAP ORF mammalian expression plasmid, N-His tag||MG50996-NH|
|Mouse FAP ORF mammalian expression plasmid, N-Myc tag||MG50996-NM|
|Mouse FAP ORF mammalian expression plasmid, N-HA tag||MG50996-NY|
|Mouse FAP natural ORF mammalian expression plasmid||MG50996-UT|
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Seprase, also known as 170 kDa melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to the peptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 170-kDa dimer, consisting of two 97-kDa subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.