Recombinant Human GPC1 Protein (N-6His)

Name: Recombinant Human GPC1 Protein (N-6His)
Brand: Beta LifeScience
SKU: BL-1079NP
Availability: InStock

BL-1079NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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Product Overview

Description	Recombinant Human Glypican-1 is produced by our Mammalian expression system and the target gene encoding Asp24-Thr529 is expressed with a 6His tag at the N-terminus.
Accession	P35052
Synonym	Glypican-1; GPC1
Gene Background	The Glypicans are a small multigene family of GPI-linked proteoglycans that play a key role in growth factor signaling. Human Glypican 1 (GPC1) is synthesized as a 558 amino acid (aa) preproprecursor that contains a 23 aa signal sequence, a 507 aa mature segment, and a 28 aa C-terminal prosegment. There are two potential N-linked and four potential O-linked sites for glycosylation or glycanation. There are potentially two heparan sulfate (HS) modifications on GPC1 that could contribute to a native molecular weight of approximately 200 kDa. Mature human GPC1 shares 91% aa identity with mature mouse GPC1. Cells known to express GPC1 include neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumorassociated vascular endothelial cells. The function of GPC1 is complex and varied. As a proteoglycan, it appears to make use of its HS adduct to impact select growth factor activity. This is accomplished by having juxtramembrane HS attachment sites, and a flexible, GPI-linkage.
Molecular Mass	57.7 KDa
Apmol Mass	65-70 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. 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: Hs.328232
Associated Diseases	Associates (via the heparan sulfate side chains) with fibrillar APP amyloid-beta peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain (PubMed:15084524).

Gene Functions References

High GPC1 expression is associated with uterine cervical cancer. 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

FAQs

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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.

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