form
lyophilized powder
specific activity
≥5 units/mg protein
composition
Protein, ~40% Bradford
storage temp.
−20°C
Quality Level
Physical form
Lyophilized powder containing Tris buffer salt
Other Notes
One unit will produce 1.0 μmole of choline from L-α-glycerophosphorylcholine, G4007, per min at pH 8.0 at 37 °C.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
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J Mitra et al.
International journal of andrology, 15(4), 345-354 (1992-08-01)
The functional interaction of the estrogen-induced uterine enzyme glycerylphosphorylcholine (GPC) diesterase with epididymal rat sperm before and after incubation under capacitating conditions was investigated indirectly, by measuring the glycerol phosphate (GP) released on enzymatic hydrolysis of GPC and using oxygen
D E Sok et al.
Neurochemical research, 20(2), 151-157 (1995-02-01)
Inhibition of a Zn(2+)-glycerophosphocholine cholinephosphodiesterase by thiols or tellurites were examined mechanistically. Inactivation of the phosphodiesterase by thio-carboxylates, which was due to the removal of Zn2+ in the catalytic site, was enhanced by introduction of an amino group in the
J P Galons et al.
Magnetic resonance in medicine, 33(3), 422-426 (1995-03-01)
The purpose of this study was to study the metabolic events during a slow acidosis in three different cell lines by combining 31P magnetic resonance spectroscopy and hollow fiber bioreactor technology. The rate of change in intracellular pH, glycerophosphorylcholine (GPC)
Carmelina D Anfuso et al.
Lipids, 38(1), 45-52 (2003-04-03)
In pericytes from bovine retina, the enzyme glycerophosphocholine phosphodiesterase, catalyzing the hydrolysis of sn-glycero-3-phosphocholine to glycero-3-phosphate and choline, has been characterized with respect to pH optimum, metal ion dependence, Km, inhibitors, and subcellular localization. In these cells, the natural substrate
Mária Simocková et al.
The Journal of biological chemistry, 283(25), 17107-17115 (2008-04-25)
The product of the open reading frame YPL206c, Pgc1p, of the yeast Saccharomyces cerevisiae displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases. Deletion of PGC1 causes an accumulation of the anionic phospholipid, phosphatidylglycerol (PG), especially under conditions of inositol limitation.
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