Mouse GLIPR1 / RTVP1 (His Tag) recombinant protein

Mouse GLIPR1 / RTVP1 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

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.

GLI pathogenesis-related 1 (Glioma)

RTVP1; CRISP7; 2410114O14RIK; GLIPR; MRTVP-1; GLIPR 1; GLIPR1; RTVP-1

Q9CWG1

Glipr1; mCG_141676

Human Cells

A DNA sequence encoding the mouse GLIPR1 (NP_082884.1) (Met1-Thr223) was expressed with a C-terminal polyhistidine tag.

Mouse

The recombinant mouse GLIPR1 comprises 217 amino acids and has a predicted molecular mass of 25.1 kDa. The apparent molecular mass of the protein is approximately 28-32 kDa in SDS-PAGE under reducing conditions.

> 85 % as determined by SDS-PAGE