Human GLIPR1 / RTVP1 (His Tag) recombinant protein

Human 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.

Glioma pathogenesis-related protein 1

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

P48060

GLIPR1; GLIPR; RTVP1

Human Cells

A DNA sequence encoding the human GLIPR1 (NP_006842.2) extracellular domain (Met 1-Arg 232) was expressed, with a C-terminal polyhistidine tag.

Human

The secreted recombinant human GLIPR1 comprises 222 amino acids and has a predicted molecular mass of 25.7 kDa. rhGLIPR1 migrates as an approximately 27 kDa band in SDS-PAGE under reducing conditions.

> 97 % as determined by SDS-PAGE