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I0274
myo-Inositol Monophosphatase from bovine brain
lyophilized powder, 5-20 units/mg protein
Synonym(e):
myo-Inositol monophosphate phosphohydrolase
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Über diesen Artikel
form
lyophilized powder
specific activity
5-20 units/mg protein
composition
Protein, ~0.5% Bradford
storage temp.
−20°C
Application
The enzyme plays a critical role in the recycling of inositol to phosphoinositides in the mammalian brain and participates in the phosphatidylinositol signaling pathway. It is inhibited non-competitively by Li+, which may be significant in the treatment of manic depression. The enzyme may help in identifying less toxic substitutes for lithium in manic depressive therapy.
Physical form
Lyophilized powder containing HEPES buffer salts, pH 7.5, and stabilizer
Other Notes
One unit will form 1.0 μmole of phosphate from inositol 1-phosphate per min at pH 7.4 at 37°C.
Lagerklasse
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Verwandter Inhalt
Datasheet
A Gupta et al.
The pharmacogenomics journal, 12(4), 328-341 (2011-03-09)
The overall neurobiological mechanisms by which lithium and valproate stabilize mood in bipolar disorder patients have yet to be fully defined. The therapeutic efficacy and dissimilar chemical structures of these medications suggest that they perturb both shared and disparate cellular
Livia Pasquali et al.
Behavioural pharmacology, 21(5-6), 473-492 (2010-08-12)
This is a short overview focusing on the biochemical interactions underlying the protective effects of lithium at the neuronal level. These include lithium modulation of autophagy, growth factors, excitotoxicity, and a variety of mechanisms underlying cell death, neurogenesis, and neuronal
Sudipta Bhattacharyya et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 4), 471-474 (2011-04-21)
The gene product of the sas2203 ORF of Staphylococcus aureus MSSA476 encodes a 30 kDa molecular-weight protein with a high sequence resemblance (29% identity) to tetrameric inositol monophosphatase from Thermotoga maritima. The protein was cloned, expressed, purified to homogeneity and crystallized.