Sf9, Baculovirus cells.
Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.
Greater than 90.0% as determined by SDS-PAGE.
GPC3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 544 amino acids (25-559a.a.) and having a molecular mass of 61.8kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GPC3 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Glypican 3, Intestinal Protein OCI-5, Glypican Proteoglycan 3, GTR2-2, MXR7, Heparan Sulphate Proteoglycan, Secreted Glypican-3, Glypican-3, OCI-5, SGBS1, DGSX, SGBS, SDYS, OCI5, SGB, GPC3.
Sf9, Baculovirus cells.
ADPQPPPPPP DATCHQVRSF FQRLQPGLKW VPETPVPGSD LQVCLPKGPT CCSRKMEEKY QLTARLNMEQ LLQSASMELK FLIIQNAAVF QEAFEIVVRH AKNYTNAMFK NNYPSLTPQA FEFVGEFFTD VSLYILGSDI NVDDMVNELF DSLFPVIYTQ LMNPGLPDSA LDINECLRGA RRDLKVFGNF PKLIMTQVSK SLQVTRIFLQ ALNLGIEVIN TTDHLKFSKD CGRMLTRMWY CSYCQGLMMV KPCGGYCNVV MQGCMAGVVE IDKYWREYIL SLEELVNGMY RIYDMENVLL GLFSTIHDSI QYVQKNAGKL TTTIGKLCAH SQQRQYRSAY YPEDLFIDKK VLKVAHVEHE ETLSSRRREL IQKLKSFISF YSALPGYICS HSPVAENDTL CWNGQELVER YSQKAARNGM KNQFNLHELK MKGPEPVVSQ IIDKLKHINQ LLRTMSMPKG RVLDKNLDEE GFESGDCGDD EDECIGGSGD GMIKVKNQLR FLAELAYDLD VDDAPGNSQQ ATPKDNEIST FHNLGNVHHH HHHH.
GPC3 is composed of a core protein to which heparan sulfate chains are attached. The protein undergoes endoproteolytic processing by proprotein convertases, resulting in multiple peptides that remain associated via disulfide bonds . The predicted molecular mass of GPC3 is approximately 61.6 kDa, but it appears as a smear with an apparent molecular mass of 60-100 kDa under non-reducing conditions in SDS-PAGE .
GPC3 is involved in modulating the activity of growth factors, such as fibroblast growth factors (FGFs), by binding to them and influencing their interaction with their receptors . This interaction is crucial for various cellular processes, including proliferation, differentiation, and migration.
GPC3 is highly expressed in hepatocellular carcinoma (HCC) and is rarely found in normal liver tissues, making it a valuable diagnostic and therapeutic target for HCC . Its overexpression in HCC and other cancers, such as melanoma, highlights its potential as a biomarker for cancer diagnosis and treatment .
Recombinant human GPC3 is produced using various expression systems, including mouse myeloma cell lines (NS0-derived). The recombinant protein is often tagged with a His-tag for purification purposes and is available in both carrier-free and carrier-containing formulations . The carrier protein, typically bovine serum albumin (BSA), enhances protein stability and shelf-life .
The recombinant GPC3 protein is used in research to study its binding interactions, particularly with growth factors like FGF. It is also utilized in the development of diagnostic and therapeutic agents targeting GPC3-expressing tumors .
Recent studies have focused on developing GPC3-specific binding peptides for imaging and therapeutic purposes. For instance, a two-step phage display screening approach identified a GPC3-specific binding peptide, TJ12P2, which shows promise as a PET imaging probe for accurate HCC diagnosis . Such advancements underscore the potential of GPC3 in cancer research and treatment.