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Human Polyclonal GPC1 Primary Antibody für ELISA, WB - ABIN561095
Payne, Jones, Chen, Zhuang: Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands. in Traffic (Copenhagen, Denmark) 2007
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Human Polyclonal GPC1 Primary Antibody für IHC, IHC (p) - ABIN4314969
Knelson, Gaviglio, Nee, Starr, Nixon, Marcus, Blobe: Stromal heparan sulfate differentiates neuroblasts to suppress neuroblastoma growth. in The Journal of clinical investigation 2014
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Human Polyclonal GPC1 Primary Antibody für FACS, WB - ABIN4899832
Koo, Dewey, García-Cardeña: Hemodynamic shear stress characteristic of atherosclerosis-resistant regions promotes glycocalyx formation in cultured endothelial cells. in American journal of physiology. Cell physiology 2013
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Human Polyclonal GPC1 Primary Antibody für IHC - ABIN966218
David, Lories, Decock, Marynen, Cassiman, Van den Berghe: Molecular cloning of a phosphatidylinositol-anchored membrane heparan sulfate proteoglycan from human lung fibroblasts. in The Journal of cell biology 1991
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Human Polyclonal GPC1 Primary Antibody für CyTOF, FACS - ABIN4899833
Hara, Takahashi, Serada, Fujimoto, Ohkawara, Nakatsuka, Harada, Nishigaki, Takahashi, Nojima, Miyazaki, Makino, Kurokawa, Yamasaki, Miyata, Nakajima, Takiguchi, Morii, Mori, Doki, Naka: Overexpression of glypican-1 implicates poor prognosis and their chemoresistance in oesophageal squamous cell carcinoma. in British journal of cancer 2016
Dynamic changes in syndecan-4- and glypican-1-positive satellite cells indicate that they are differentially expressed during myogenesis.
Glypican-1 regulates myogenic differentiation when it is shed into the extracellular matrix.
These data suggested that expression of the myogenic regulatory transcription factors are dependent upon expression of glypican-1 and syndecan-4 during satellite cell proliferation and differentiation, and Pax7 expression is influenced by glypican-1.
These data suggest that glypican-1 N-glycosylated chains and GAG chains are critical in regulating turkey myogenic satellite cell proliferation, differentiation, and responsivness to FGF2.
syndecan-1, syndecan-4, or glypican-1 differentially affect the processes of turkey muscle cell proliferation and differentiation, and can regulate these developmental stages in an FGF2-independent manner
High GPC1 expression is associated with uterine cervical cancer.
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.
Glypican-1 was validated as a novel substrate for ADAM17, with important function in adhesion, proliferation and migration of carcinoma cells.
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.
The role of glypican-1 in mediating the eNOS activation under shear stress might involve in protecting the endothelial function against disturbed flow.
independent case-control study implicated that common SNPs in GPC1 gene contributed to biliary atresia susceptibility in Chinese population
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.
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
differences in expression among different subtypes of ameloblastomas
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.
GPC1 and FGFR1 are targets for regulation of their gene expression by miR-149.
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.
We now report that human primary suture mesenchymal cells coexpress GPC1 and GPC3 on the cell surface and release them into the media
Crystal structure of N-glycosylated human glypican-1 core protein shows the structure of two loops evolutionarily conserved in vertebrate glypican-1
High glucose can decrease the expression of core protein Sydecan-1 and Glypican-1 in cultured human renal glomerular endothelial cells.
Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
The N-unsubstituted glucosamine residues are formed during biosynthesis of glypican-1 and the content increased upon inhibition of polyamine synthesis.
Augmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophy.
S-nitrosylation and Copper-dependent autocleavage of glypican 1
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
This study provides new insights into the roles of GPC1 and GPC3 in mandibular morphogenesis. GPC3-knockout reduces mandibular growth, but GPC1 does not. These findings along with previous studies indicate that glypicans could be potential therapeutic agents to manage craniosynostosis and associated bony dysmorphology.
Amyloid precursor protein (APP)/APP-like protein 2 (APLP2) expression is required to initiate endosome-nucleus-autophagosome
The N-terminal growth-factor-like domain of amyloid-beta precursor protein is necessary for protein-receptor binding, whereas the E2-domain mediates interaction with membrane-anchored syndecan 2 and glypican 1.
Glypican-1 is expressed by neural stem cells and neurons derived from embryonic stem cells, which are then surrounded with cell bodies and processes, which in certain cases show distinctive expression patterns.
Glypican-1 is a novel cellular cofactor for prion conversion. It acts as a scaffold facilitating the interaction of PrP(C) and PrP(Sc) in lipid rafts.
data imply that endogenous Gpc1 is involved in control of growth factor signaling, a finding that is both novel and relevant to the general question of how the activities of co-receptors are exploited during development
glypican-1 core protein has a specific role in FGF2 signaling. Glypican-1 overexpression may contribute to angiogenesis and the radiation resistance characteristic of this malignancy.
Data describe a relationship between heparan sulfate and copper binding of amyloid precursor protein (APP) and amyloid precursor-like protein 2 (APLP2) in the modulation of nitroxyl anion-catalyzed heparan sulfate degradation in glypican-1.
cancer cell- and host-derived GPC1 are crucial for full mitogenic, angiogenic, and metastatic potential of cancer cells
GPC1 regulates EC cell cycle progression at least partially by modulating APC/C-mediated degradation of mitotic cyclins and securin
These results suggest a role for Gpc-1 autoprocessing in the clearance of PrP(Sc) from infected cells.
GPC1 may have an important role in the establishment of a microenvironment that supports early events in hematopoiesis.
Heparan sulfate is involved in both centralized and decentralized glycocalyx-mediated mechanotransduction, with GPC1 acting as a centralized agent and SDC1 functioning in decentralized mechanotransmission. GPC1 mediates NOS3 activation.
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation.
, glypican proteoglycan 1
, GPI-anchored cell surface heparan sulfate proteoglycan
, heparan sulfate proteoglycan core protein