Recombinant Human Glypican 1/ GPC1 protein (GST tag N-Terminus)
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Recombinant Human Glypican 1/ GPC1 protein (GST tag N-Terminus) is a Human Fragment protein, in the 24 to 131 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Glypican-1, GPC1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Glypican 1/ GPC1 protein (GST tag N-Terminus) (AB114484)
12.5% SDS-PAGE showing ab114484 at approximately 37.51kDa stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GPC1 influences the regulation of growth factors and morphogens and it has a significant role in the cell division and growth processes. It is not recognized as part of any larger protein complex but interacts with diverse ligand molecules. Researchers identify GPC1 as an important facilitator of fibroblast growth factors (FGF) and sonic hedgehog (Shh) signaling. Its interaction with molecular partners helps to regulate developmental signals important for proper cellular function and organ development.
Pathways
The contributions of GPC1 are observed in the hedgehog signaling pathway and fibroblast growth factor signaling. GPC1's interaction within the hedgehog pathway is critical for organizing cellular growth and differentiation while its involvement in the FGF pathway supports angiogenesis and wound healing. GPC1 coordinates with other glypican family members and related proteins like FGFR1 to mediate these signaling processes effectively.
Specifications
Form
Liquid
General info
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 (By similarity). 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.
Sequence similarities
Belongs to the glypican family.
Post-translational modifications
S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.. N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts.. This cell-associated glypican is further processed to give rise to a medium-released species.
Subcellular localisation
Endosome
Target data
Product promise
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