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Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Additionally we are shipping Glypican 1 Kits (42) and Glypican 1 Proteins (12) and many more products for this protein.
Showing 10 out of 79 products:
Human Polyclonal GPC1 Primary Antibody for ELISA, WB - ABIN561095
Payne, Jones, Chen, Zhuang: Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands. in Traffic (Copenhagen, Denmark) 2007
Show all 2 references for ABIN561095
Human Polyclonal GPC1 Primary Antibody for EIA, FACS - ABIN952553
Sjöblom, Jones, Wood, Parsons, Lin, Barber, Mandelker, Leary, Ptak, Silliman, Szabo, Buckhaults, Farrell, Meeh, Markowitz, Willis, Dawson, Willson, Gazdar, Hartigan, Wu, Liu, Parmigiani, Park et al.: The consensus coding sequences of human breast and colorectal cancers. ... in Science (New York, N.Y.) 2006
Dog (Canine) Polyclonal GPC1 Primary Antibody for EIA, WB - ABIN401059
Bianco, Strizzi, Rehman, Normanno, Wechselberger, Sun, Khan, Hirota, Adkins, Williams, Margolis, Sanicola, Salomon: A Nodal- and ALK4-independent signaling pathway activated by Cripto-1 through Glypican-1 and c-Src. in Cancer research 2003
Dynamic changes in syndecan-4 (show SDC4 Antibodies)- 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 (show SDC4 Antibodies) during satellite cell proliferation and differentiation, and Pax7 (show PAX7 Antibodies) 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 (show FGF2 Antibodies).
syndecan-1 (show SDC1 Antibodies), syndecan-4 (show SDC4 Antibodies), or glypican-1 differentially affect the processes of turkey muscle cell proliferation and differentiation, and can regulate these developmental stages in an FGF2 (show FGF2 Antibodies)-independent manner
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
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 (show FGFR1 Antibodies) are targets for regulation of their gene expression by miR (show MLXIP Antibodies)-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 (show GPC3 Antibodies) 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.
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 (show DMD Antibodies).
S-nitrosylation and Copper-dependent autocleavage of glypican 1
Amyloid precursor protein (APP)/APP-like (show APP Antibodies) protein 2 (APLP2 (show APLP2 Antibodies)) 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 (show SDC2 Antibodies) 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 (show PRNP Antibodies) conversion. It acts as a scaffold facilitating the interaction of PrP(C (show PRNP Antibodies)) 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 (show FGF2 Antibodies) 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 (show APP Antibodies)) and amyloid precursor-like protein 2 (APLP2 (show APLP2 Antibodies)) 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 (show APC Antibodies)/C-mediated degradation of mitotic cyclins and securin (show PTTG1 Antibodies)
These results suggest a role for Gpc-1 autoprocessing in the clearance of PrP(Sc) from infected cells.
Heparan sulfate is involved in both centralized and decentralized glycocalyx-mediated mechanotransduction, with GPC1 acting as a centralized agent and SDC1 (show SDC1 Antibodies) functioning in decentralized mechanotransmission. GPC1 mediates NOS3 (show NOS3 Antibodies) 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