G9768
Guanosine 5′-triphosphate–Agarose
aqueous glycerol suspension
Synonym(s):
5′-GTP agarose
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About This Item
Recommended Products
biological source
bacterial (CORYNEBACTERIUM SP)
enzyme from Porcine brain
plant (Sea weed)
yeast
Quality Level
form
aqueous glycerol suspension
extent of labeling
1-5 μmol per mL
matrix
cross-linked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
ribose hydroxyls
matrix spacer
11 atoms (adipic acid dihydrazide)
storage temp.
−20°C
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Application
Guanosine 5′-triphosphate-agarose (5′-GTP agarose) is an agarose conjugate in aqueous glycerol suspension used in affinity chromatography, for purification of guanosine-binding proteis
Physical form
Guanosine 5′-triphosphate–Agarose has been used:
- in chromatographic column for the purification of a translocation stimulating factor
- in GTP-Agarose pull down assays to measure the levels of GTP-bound RHEB (Ras homolog enriched in brain)
- in GTP-Binding assay
- for the depletion of GTP binding proteins in cytosol of rat liver
Suspension in 50% glycerol containing 0.25 M NaCl
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
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Molecular and biochemical parasitology, 65(2), 233-245 (1994-06-01)
The hypoxanthine-guanine phosphoribosyltransferase (HGPRT) enzyme in Trypanosoma cruzi is a rational target for the treatment of Chagas disease. To evaluate the T. cruzi HGPRT in detail, the HGPRT gene (hgprt) was cloned from a genomic library of T. cruzi DNA
Possible role of both the alpha and beta gamma subunits of the heterotrimeric G protein, Gs, in transcytosis of the polymeric immunoglobulin receptor
The Journal of Biological Chemistry, 268, 25824-25835 (1993)
70K heat shock related proteins stimulate protein translocation into microsomes
Nature, 332, 805-805 (1988)
The Journal of biological chemistry, 268(34), 25824-25835 (1993-12-05)
In endosomes the polymeric immunoglobulin receptor (pIgR) is sorted into transcytotic vesicles. Transcytosis of the pIgR in polarized Madin-Darby canine kidney (MDCK) cells is regulated both by phosphorylation of Ser664 and by binding of ligand, dimeric IgA (dIgA). Mutation of
Biochemistry, 34(38), 12193-12203 (1995-09-26)
Recently we demonstrated that the unique stereoelectronic relationships inherent in the structure of plasmenylethanolamine facilitate membrane fusion, and we postulated the existence of a membrane fusion protein which could exploit the propensity of plasmenylethanolamine molecular species to adapt an inverted
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