Recombinant Human Glypican-1 (GPC1) Protein (His-GST&Myc)

Name: Recombinant Human Glypican-1 (GPC1) Protein (His-GST&Myc)
Brand: Beta LifeScience
SKU: BLC-01510P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glypican-1 (GPC1) Protein (His-GST&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P35052
Target Symbol	GPC1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-GST&C-Myc
Target Protein Sequence	GCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQKTS
Expression Range	342-530aa
Protein Length	Partial
Mol. Weight	55.7 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination. May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.
Subcellular Location	Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.; [Secreted glypican-1]: Secreted, extracellular space.
Protein Families	Glypican family
Database References	HGNC: 4449 OMIM: 600395 KEGG: hsa:2817 STRING: 9606.ENSP00000264039 UniGene: PMID: 29055044 The results demonstrated that the GPC1 gene was re-expressed in pancreatic ductal adenocarcinoma (PDAC) mainly due to promoter hypomethylation, even for early-stage PDAC. High levels of GPC1 were associated with poorer pathological differentiation and worse biological behaviors. GPC1 could serve as an independent unfavorable prognostic factor in PDAC. PMID: 28440066 Glypican-1 was validated as a novel substrate for ADAM17, with important function in adhesion, proliferation and migration of carcinoma cells. PMID: 27576135 Exosomal miR signature is superior to exosomal GPC1 or plasma CA 19-9 levels in establishing a diagnosis of pancreatic ductal carcinoma and differentiating between PDAC and chronic pancreatitis. PMID: 28232049 The role of glypican-1 in mediating the eNOS activation under shear stress might involve in protecting the endothelial function against disturbed flow. PMID: 27688027 independent case-control study implicated that common SNPs in GPC1 gene contributed to biliary atresia susceptibility in Chinese population PMID: 27373597 The C terminus is shown to be highly flexible in solution, but it orients the core protein transverse to the membrane, directing a surface evolutionarily conserved in Gpc1 orthologs toward the membrane, where it may interact with signaling molecules PMID: 26203194 differences in expression among different subtypes of ameloblastomas PMID: 25046223 GPC1(+) crExos were detected in the serum of patients with pancreatic cancer with absolute specificity and sensitivity, distinguishing healthy subjects and patients with a benign pancreatic disease in patients with early-and late-stage pancreatic cancer. PMID: 26106858 GPC1 and FGFR1 are targets for regulation of their gene expression by miR-149. PMID: 24463821 DNA from 4 HPV positive and 4 HPV negative fresh frozen primary HNSCC were subject to comprehensive genome-wide methylation profiling.Pathway analysis of 1168 methylated genes showed 8 signal transduction pathways (GPC1) of which 62% are hypermethylated. PMID: 23736812 Crystal structure of N-glycosylated human glypican-1 core protein shows the structure of two loops evolutionarily conserved in vertebrate glypican-1 PMID: 22351761 High glucose can decrease the expression of core protein Sydecan-1 and Glypican-1 in cultured human renal glomerular endothelial cells. PMID: 21265098 Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied. PMID: 21932778 The N-unsubstituted glucosamine residues are formed during biosynthesis of glypican-1 and the content increased upon inhibition of polyamine synthesis. PMID: 19479373 Augmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophy. PMID: 11968010 S-nitrosylation and Copper-dependent autocleavage of glypican 1 PMID: 12084716 inhibition of Gpc-1 expression abrogates spermine uptake and intracellular delivery; ascorbate released NO, which degraded heparan sulfate side chains and liberated the bound spermine PMID: 12972423 glypican-1 is required for efficient TGF-beta1 signaling in pancreatic cancer cells PMID: 15249209 syndecan-1 and glypican-1 have roles in progression of ovarian cancer PMID: 15297422 glypican 1 (GPC1) is deleted in both reported patients suffering from Albright hereditary osteodystrophy-like (AHO-like) syndrome PMID: 15547662 Enhanced GPC1 expression correlates with BMP and activin receptors in pancreatic cancer. PMID: 17016645 cancer cell- and host-derived GPC1 are crucial for full mitogenic, angiogenic, and metastatic potential of cancer cells PMID: 18064304 Glypican-3 can be especially useful in the identification of poorly differentiated hepatocellular carcinoma. PMID: 18536657 study concludes that Abeta can modulate the cellular expression of agrin and glypican-1, which may contribute to the accumulation of these heparan sulfate proteoglycans in Alzheimer's disease lesions PMID: 19166823

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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.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.