|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 GLIPR1 ORF mammalian expression plasmid, C-GFPSpark tag||MG50869-ACG|
|Mouse GLIPR1 ORF mammalian expression plasmid, C-OFPSpark / RFP tag||MG50869-ACR|
|Mouse GLIPR1 ORF mammalian expression plasmid, C-Flag tag||MG50869-CF|
|Mouse GLIPR1 ORF mammalian expression plasmid, C-His tag||MG50869-CH|
|Mouse GLIPR1 ORF mammalian expression plasmid, C-Myc tag||MG50869-CM|
|Mouse GLIPR1 ORF mammalian expression plasmid, C-HA tag||MG50869-CY|
|Mouse GLIPR1 Gene cDNA clone plasmid||MG50869-G|
|Mouse GLIPR1 ORF mammalian expression plasmid, N-Flag tag||MG50869-NF|
|Mouse GLIPR1 ORF mammalian expression plasmid, N-His tag||MG50869-NH|
|Mouse GLIPR1 ORF mammalian expression plasmid, N-Myc tag||MG50869-NM|
|Mouse GLIPR1 ORF mammalian expression plasmid, N-HA tag||MG50869-NY|
|Mouse GLIPR1 natural ORF mammalian expression plasmid||MG50869-UT|
|Learn more about expression Vectors|
Glioma pathogenesis-related protein 1, also known as Protein RTVP-1, GLIPR1 and GLIPR, is a single-pass membrane protein which belongs to the CRISP family. GLIPR1 / RTVP-1 was expressed in high levels in glioblastomas, whereas its expression in low-grade astrocytomas and normal brains was very low. Transfection of glioma cells with small interfering RNAs targeting GLIPR1 / RTVP-1 decreased cell proliferation in all the cell lines examined and induced cell apoptosis in some of them. Overexpression of GLIPR1 / RTVP-1 increased astrocyte and glioma cell proliferation and the anchorage-independent growth of the cells. In addition, overexpression of GLIPR1 / RTVP-1 rendered glioma cells more resistant to the apoptotic effect of tumor necrosis factor-related apoptosis-inducing ligand and serum deprivation. GLIPR1 / RTVP-1 regulated the invasion of glioma cells was evident by their enhanced migration through Matrigel and by their increased invasion in a spheroid confrontation assay. The increased invasive potential of the GLIPR1 / RTVP-1 overexpressors was also shown by the increased activity of matrix metalloproteinase 2 in these cells. The expression of GLIPR1 / RTVP-1 is correlated with the degree of malignancy of astrocytic tumors and that GLIPR1 / RTVP-1 is involved in the regulation of the growth, survival, and invasion of glioma cells. GLIPR1 / RTVP-1 is a potential therapeutic target in gliomas.