Download Recombinant Human Glypican-1 (carrier-free)

Survey
yes no Was this document useful for you?
   Thank you for your participation!

* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project

Document related concepts

Protein adsorption wikipedia , lookup

Cell culture wikipedia , lookup

Expanded genetic code wikipedia , lookup

Biochemistry wikipedia , lookup

Cell-penetrating peptide wikipedia , lookup

List of types of proteins wikipedia , lookup

Channelrhodopsin wikipedia , lookup

Transcript
Version: 2
Revision Date: 07/14/2016
Recombinant Human Glypican-1 (carrier-free)
Catalog# / Size
757202 / 10 µg
757206 / 100 µg
757204 / 25 µg
757208 / 500 µg
Other Names
GPC1, GPC-1
Ave. Rating
★★★★★ 0 reviews
Description
When human Glypican-1 is immobilized at 2
Glypicans are heparin sulfate proteoglycans that are bound to the outer cell
µg/mL, human FGF-basic binds with EC50 of 2
surface membrane by a glycosyl-phosphatidylinositol (GPI) linkage. There
- 8 ng/mL in a functional ELISA.
are six known mammalian Glypicans (GPC1 to GPC6) and they can be
released from the cell surface by a lipase called Notum. The main function
of membrane bound glypicans is to regulate the signaling of Wnts,
Hedgehogs, fibroblast growth factors, and bone morphogenetic proteins.
Glypican-1 has been associated with the tumorigenic process, mostly by
affecting growth factor signaling and cell proliferation. Glypican-1 shows
increased expression in human gliomas, and acts by enhancing fibroblast
growth factor (FGF) basic signaling and mitogenesis. Glypican-1, also known
as GPC1, is over-produced in pancreatic and breast cancer cells and has
been shown to be a marker of cancer-derived exosomes in these cancers.
GPC1 is also shown to associate with fibrillar APP Aβ peptides in lipid rafts
of Alzheimer disease brains. GPC1 is synthesized as a 558 amino acid
preproprecursor that contains a 23 amino acid signal peptide, a 507 amino
acid mature segment, and a 28 amino acid C-terminal propeptide. There
are two potential N-linked and three potential O-linked sites for glycosylation
and potentially three heparan sulfate modifications on GPC1. GPC1 is
expressed on neurons, smooth and skeletal muscle cells, keratinocytes,
osteoblasts, Schwann cells, immature dendritic cells, and tumor, plus tumorassociated vascular endothelial cells.
Source
Human Glypican-1, amino acids Asp24-Ser530 (Accession# P35052) with C-terminal TGHHH
HHHHHGGQ, was expressed in 293E cells.
Molecular Mass
The 520 amino acid recombinant protein has a predicted molecular mass of approximately
57.5 kD. The protein migrates at approximately 65 kD in DTT-reducing conditions and at
approximately 60 kD in non-reducing conditions by SDS-PAGE. The predicted N-terminal
amino acid is Asp.
Purity
>95%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS, pH 7.2.
Endotoxin Level
Less than 0.1 EU per µg protein as determined by the LAL method.
Concentration
10 - 100 µg sizes are bottled at 200 µg/mL. 500 µg and larger sizes are bottled at the
concentration indicated on the vial.
Storage & Handling
Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to
opening. Stock solutions can also be prepared at 50 - 100 µg/mL in sterile buffer (PBS, HPBS,
DPBS, or EBSS) and stored in working aliquots at -20°C to -70°C. Avoid repeated freeze/thaw
cycles.
Activity
When human Glypican-1 is immobilized at 2 µg/mL, human FGF-basic binds with EC 50 of 2 - 8
ng/mL.
Application
Bioassay
Antigen Details
Distribution
Glypican-1 is expressed on neurons, smooth and skeletal muscle cells, keratinocytes, osteoblasts,
Schwann cells, immature dendritic cells, and tumor, plus tumor-associated vascular endothelial
cells.
Function
The main function is to regulate the signaling of fibroblast growth factors.
Interaction
Fibroblast growth factors, extracellular matrix, and APP Abeta peptides.
Ligand Receptor
Fibroblast growth factors and laminin.
Bioactivity
Measured by the ability of immobilized human Glypican-1 to bind human FGF-basic in a
functional ELISA.
Antigen References
1. Kleeff J, et al. 1998. J. Clin. Invest. 102:1662-73.
2. Gengrinovitch S, et al. 1999. J. Biol. Chem. 274:10816-22.
3. Matsuda K, et al. 2001. Cancer Res. 14:5562-9.
4. Qiao D, et al. 2003. 278:16045-53.
5. Watanabe N, et al. 2004. FASEB J. 9:1013-5.
6. Bishop JR, et al. 2007. Nature 446:1030-7.
7. Aikawa T, et al. 2008. J. Clin. Invest. 118:89-99.
8. Melo SA, et al. 2015. Nature 523:177-182.
Gene ID
2817
UniProt
View information about Glypican-1 on UniProt.org
Documentation
Technical data sheet
Certificate of Analysis
Safety Data Sheet
Related FAQs
How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
Related Categories
Cytokines & Chemokines > Human Cytokine & Chemokine Research > Recombinant Proteins > Glypican-1 >
Cytokines & Chemokines > RecombinantProteins > Human > Glypican-1 >
NeuroscienceProducts > Synaptic Biology > Synaptic Biology Recombinant Proteins >
For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or
other violations that may occur with the use of our products.
*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website,
www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or
used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties
without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited
Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or
animal diagnostic, therapeutic or commercial use.
BioLegend Inc., 9727 Pacific Heights Blvd, San Diego, CA 92121 www.biolegend.com
Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587