Biotinylated Human GPC3 Protein (C-6His-Avi)

Name: Biotinylated Human GPC3 Protein (C-6His-Avi)
Brand: Beta LifeScience
SKU: BL-2404NP
Availability: InStock

BL-2404NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Antibody / cell therapy targets, Avi-tagged proteins, Biotinylated proteins, Car-nk targets proteins, Car-t cell therapy targets, Featured biotinylated protein molecules, Recombinant proteins

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Product Overview

Description	Biotinylated Recombinant Human Glypican-3 is produced by our Mammalian expression system and the target gene encoding Gln25-His559 is expressed with a 6His, Avi tag at the C-terminus.
Accession	P51654
Synonym	Glypican-3; GTR2-2; Intestinal protein OCI-5; MXR7; GPC3; OCI5
Gene Background	Glypican-3/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.
Molecular Mass	63.4 KDa
Apmol Mass	60-180&36-44 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Cell surface proteoglycan that bears heparan sulfate. Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins. Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation. Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands. Positively regulates the non-canonical Wnt signaling pathway. Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression. Inhibits the dipeptidyl peptidase activity of DPP4. Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4. Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis. Required for coronary vascular development. Plays a role in regulating cell movements during gastrulation.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
Protein Families	Glypican family
Database References	HGNC: 4451 OMIM: 300037 KEGG: hsa:2719 STRING: 9606.ENSP00000377836 UniGene: Hs.644108
Associated Diseases	Simpson-Golabi-Behmel syndrome 1 (SGBS1)
Tissue Specificity	Highly expressed in lung, liver and kidney.

Gene Functions References

The areas under the receiver operating curve (AUROC) value, sensitivity and specificity of glypican 3 (GPC3) for hepatoblastoma (HB) pretreatment group versus all controls were all significantly lower than those of alpha-fetoprotein (AFP). PMID: 28378832
GPC3 is operating through an intricate molecular signaling network. From the balance of these interactions, the inhibition of breast metastatic spread induced by GPC3 emerges. PMID: 30267212
Its surface is modified with anti-GPC3 antibody. PMID: 29916268
data suggest that transcriptionally targeted delivery of transgene in HCC cells can be achieved using the GPC3 promoter and this targeting strategy produces limited toxicity to normal liver cells PMID: 29563582
High GPC3 expression is associated with Hepatocellular Carcinoma. PMID: 28429175
Study demonstrated that GPC3 expression is inversely associated with glucose metabolism, suggesting that GPC3 may play a role in regulating glucose metabolism in hepatocellular carcinoma. PMID: 29398870
the intravenous injection of SF-PL/siGPC3 into nude mice bearing subcutaneous human HepG2 xenografts effectively inhibited tumor growth and also increased the survival rates of animals. These results revealed the great potential of the PEI-modified liposomal nanomedicine carrying SF and siGPC3 to improve Hepatocellular carcinomatreatment PMID: 29106433
Invasive hepatocellular carcinoma (HCC) samples and HCC cell lines with high metastatic potential exhibited higher MXR7 expression. Overexpression of MXR7 promoted epithelial-mesenchymal transition (EMT) progress, and MXR7 depletion repressed the EMT phenotype. Human MXR7 protein is a mediator of EMT and metastasis in HCC. PMID: 28812296
Overexpression of GPC3 was significantly associated with poor prognosis in patients with hepatocellular carcinoma. PMID: 29901640
These data show that glycanation and convertase maturation are not required for soluble mutant GPC3 to inhibit hepatocellular carcinoma cell proliferation. PMID: 29345911
Data indicate that several microRNAs targeting the oncogenic functions of glypican-3 (GPC3). PMID: 28476031
presence distinguishes aggressive from non-aggressive odontogenic tumors PMID: 27647326
GPC3 as a potential metastasis suppressor gene and suggest its value as a prognostic marker in gastric cancer. PMID: 27259271
In this study we systematically evaluated a series of CAR constructs targeting glypican-3 (GPC3), which is selectively expressed on several solid tumors. We compared GPC3-specific CARs that encoded CD3zeta (Gz) alone or with costimulatory domains derived from CD28 (G28z), 4-1BB (GBBz), or CD28 and 4-1BB (G28BBz). PMID: 27530312
Data indicate that glypican-3 (GPC3) is an important regulator of epithelial-mesenchymal transition (EMT) in breast cancer, and a potential target for procedures against breast cancer metastasis. PMID: 27507057
Glypican-3 overexpression in Wilms tumor correlates with poor overall survival. PMID: 28432433
glypican-3 has a role in HBV-related hepatocellular carcinoma PMID: 27286460
MOSPD1 is a possible candidate gene for DORV, probably in combination with GPC3. Further studies of the combined functions of MOSPD1 and GPC3 are needed, and identification of additional patients with MOSPD1 and GPC3 duplication should be pursued PMID: 28636109
Glypican-3 is correlated with the clinical malignant behavior of hepatocellular carcinoma and its phenotype changes from positive to negative during tumor cells differentia- tion. PMID: 28087980
The diagnostic sensitivity for hepatocellular carcinoma increased to 72.8% (206 of the 283) when glypican 3 was combined with alpha-fetoprotein. PMID: 26370140
The lncRNA glypican 3 antisense transcript 1 (GPC3-AS1) has been reported to be a potential biomarker for hepatocellular carcinoma (HCC) screening. We observed a significant upregulation of GPC3-AS1 in HCC. Increased expression of GPC3-AS1 was associated with alpha-fetoprotein, tumor size, microvascular invasion, encapsulation, Barcelona Clinic Liver Cancer stage, and worse prognosis of HCC patients. PMID: 27573079
study provides the first evidence that GPC3 can modulate the PCSK9 extracellular activity as a competitive binding partner to the LDLR in HepG2 cells. PMID: 27758865
By subsequent Sanger sequencing of genomic DNA we could map the chromosomal break points to define a deletion size of 43,617 bp including exons 5 and 6 of the GPC3 gene. PMID: 28371070
This is the first study in which the optimal HLA-A*0201 GPC3 epitopes were screened from a large number of candidates predicted by three software. The optimized HLA-A*0201 GPC3 peptides will provide new epitope candidates for hepatocellular carcinoma (HCC) immunotherapy. PMID: 27102087
GPC3 and KRT19 overexpression are associated with carcinogenesis, progression, and poor prognosis in patients with PDAC and a valuable biomarker for diagnosis of PDAC. PMID: 27689616
The clinical implication of GPC3 detection and targeting in the management of patients with hepatocellular carcinoma. Review. PMID: 26755876
Glypican 3 expression showed a significant difference between endometrioid endometrial carcinoma and serous endometrial carcinoma, and it was significantly correlated with tumor grade, stage and myometrial invasion PMID: 26722522
Data show that notum and glypican-1 and glypican-3 gene expression during colorectal cancer (CRC) development and present evidence to suggest them as potential new biomarkers of CRC pathogenesis. PMID: 26517809
GPC3 expression was measured in hepatocellular carcinoma at different stages and correlated with prognosis. CK19+/GPC3+ HCC has the highest risk of intrahepatic metastasis, microvascular invasion, regional lymph node involvement, and distant metastasis. PMID: 26977595
Review: Glypican-3 is a highly specific biomarker for the diagnosis of hepatocellular carcinoma and a promising therapeutic target. PMID: 26256079
In South Korean hepatocellular carcinoma patients, GPC3 expression was more frequent in hepatocellular carcinoma with aggressive features, but it was not an independent prognostic biomarker. PMID: 26764243
In this meta-analysis, GPC3 was found to be acceptable as a serum marker for the diagnosis of hepatocellular carcinoma. PMID: 26502856
GPC3 may be a candidate marker for detecting lung squamous cell carcinoma. PMID: 26345955
study suggests that GPC3 is involved in HCC cell migration and motility through HS chain-mediated cooperation with the HGF/Met pathway, showing how HS targeting has potential therapeutic implications for liver cancer PMID: 26332121
potential role of GPC3 in urothelial carcinogenesis warrants further investigation, especially the potential use of Glypican-3 for therapeutic and diagnostic purposes PMID: 25896897
Downregulation of glypican-3 expression increases migration, invasion, and tumorigenicity of ovarian cancer. PMID: 25967456
GPC3 expression is an independent prognostic factor for postoperative hepatocellular carcinoma PMID: 25432695
Identify a GPC3-specific T-cell receptor. Expression of this receptor by T cells allows them to recognize and kill GPC3-positive hepatoma cells. PMID: 26052074
High expression of glypican-3 is associated hepatoblastoma. PMID: 25735325
GPC3 and E-cadherin expressions are not independent prognostic factors in CRC. PMID: 25619476
In HCC patients, sGPC3N levels were significantly increased (mean/median, 405.16/236.19 pg mL(-1) ) compared to healthy controls (p < 0.0001), and 60% of HCC cases (69/115) showed sGPC3N levels that were higher than the upper normal limit. PMID: 25784484
GPC3 contributes to hepatocellular carcinoma progression and metastasis through impacting epithelial-mesenchymal transition of cancer cells, and the effects of GPC3 are associated with ERK activation. PMID: 25572615
Most cases of hepatoblastoma and yolk sac tumor, and some cases of other tumors were found to express GPC3. On the other hand, GPC3 was physiologically expressed during the fetal and neoinfantile period under 1 year of age. PMID: 25344940
OPN, SPINK1, GPC3 and KNPA2 were significantly over-expressed in HCC tissues. These genes may be useful in developing future biomarkers and therapeutic strategies for HCC PMID: 25862856
Data indicate that zinc-fingers and homeoboxes 2 (ZHX2) suppresses glypican 3 (GPC3) transcription by binding with its core promoter. PMID: 25195714
propose that the structural changes generated by the lack of cleavage determine a change in the sulfation of the HS chains and that these hypersulfated chains mediate the interaction of the mutant GPC3 with Ptc PMID: 25653284
GPC3 is associated with the HCC cell biological behavior. PMID: 25270552
Data indicate that the triple stain of reticulin, glypican-3, and glutamine synthetae is useful in the differentiation of hepatocellular carcinoma, hepatic adenoma, and focal nodular hyperplasia. PMID: 25822763
Data shows that GPC3 gene expression is downregulated in primary clear cell renal cell carcinoma; its overexpression arrest cells in G1 phase suggesting its role as tumor suppressor in clear cell renal cell carcinoma. PMID: 25168166
This study demonstrated that highly expression of GPC3 could enrich hepatocellular carcinoma -related genes' mRNA expression and positive associate with dysplasia in cirrhotic livers. PMID: 25542894

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

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Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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