Catalogue Number
AV-C10166
Analysis Method
HPLC,NMR,MS
Specification
98%
Storage
2-8°C
Molecular Weight
344.3
Appearance
Yellow powder
Botanical Source
Structure Type
Flavonoids
Category
Standards;Natural Pytochemical;API
SMILES
COC1=CC=C(C=C1)C2=C(C(=O)C3=C(O2)C(=C(C=C3O)O)OC)OC
Synonyms
5,7-Dihydroxy-3,4',8-trimethoxyflavone/5,7-Dihydroxy-3,8,4'-trimethoxyflavone/4H-1-Benzopyran-4-one, 5,7-dihydroxy-3,8-dimethoxy-2-(4-methoxyphenyl)-/W1654/3,8,4'-Trimethylherbacetin/5,7-Dihydroxy-3,8-dimethoxy-2-(4-methoxyphenyl)-4H-chromen-4-one/Herbacetin 3,8,4'-trimethyl ether
IUPAC Name
5,7-dihydroxy-3,8-dimethoxy-2-(4-methoxyphenyl)chromen-4-one
Density
1.5±0.1 g/cm3
Solubility
mild hypothermia, mathematical modeling, CHO cells, N?linked glycosylation, galactosylation, flux balance analysis, monoclonal antibody
Flash Point
212.2±23.6 °C
Boiling Point
577.3±50.0 °C at 760 mmHg
Melting Point
InChl
InChl Key
RXQVMRRNRHSOTC-UHFFFAOYSA-N
WGK Germany
RID/ADR
HS Code Reference
2932990000
Personal Projective Equipment
Correct Usage
For Reference Standard and R&D, Not for Human Use Directly.
Meta Tag
provides coniferyl ferulate(CAS#:1570-09-8) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
No Technical Documents Available For This Product.
27869292
Despite the positive effects of mild hypothermic conditions on monoclonal antibody (mAb) productivity (q mAb) during mammalian cell culture, the impact of reduced culture temperature on mAb Fc?glycosylation and the mechanism behind changes in the glycan composition are not fully established. The lack of knowledge about the regulation of dynamic intracellular processes under mild hypothermia restricts bioprocess optimization. To address this issue, a mathematical model that quantitatively describes Chinese hamster ovary (CHO) cell behavior and metabolism, mAb synthesis and mAb N?linked glycosylation profile before and after the induction of mild hypothermia is constructed. Results from this study show that the model is capable of representing experimental results well in all of the aspects mentioned above, including the N?linked glycosylation profile of mAb produced under mild hypothermia. Most importantly, comparison between model simulation results for different culture temperatures suggests the reduced rates of nucleotide sugar donor production and galactosyltransferase (GalT) expression to be critical contributing factors that determine the variation in Fc?glycan profiles between physiological and mild hypothermic conditions in stable CHO transfectants. This is then confirmed using experimental measurements of GalT expression levels, thereby closing the loop between the experimental and the computational system. The identification of bottlenecks within CHO cell metabolism under mild hypothermic conditions will aid bioprocess optimization, for example, by tailoring feeding strategies to improve NSD production, or manipulating the expression of specific glycosyltransferases through cell line engineering. Biotechnol. Bioeng. 2017;114: 1570-1582. ? 2016 The Authors. Biotechnology and Bioengineering Published by Wiley Periodicals Inc.
mild hypothermia, mathematical modeling, CHO cells, N?linked glycosylation, galactosylation, flux balance analysis, monoclonal antibody
Model?based investigation of intracellular processes determining antibody Fc?glycosylation under mild hypothermia
Si Nga Sou, 1 , 2 , 3 Philip M. Jedrzejewski, 3 Ken Lee, 4 Christopher Sellick, 4 Karen M. Polizzi, 1 , 2 and Cleo Kontoravdicorresponding author 3
2017 Jul;
7929833
Insulin-mediated vasodilation has been proposed as a determinant of in vivo insulin sensitivity. We tested whether sustained vasodilation with adenosine could overcome the muscle insulin resistance present in mildly overweight patients with essential hypertension. Using the forearm technique, we measured the response to a 40-min local intraarterial infusion of adenosine given under fasting conditions (n = 6) or superimposed on a euglycemic insulin clamp (n = 8). In the fasting state, adenosine-induced vasodilation (forearm blood flow from 2.6 +/- 0.6 to 6.0 +/- 1.2 ml min-1dl-1, P < 0.001) was associated with a 45% rise in muscle oxygen consumption (5.9 +/- 1.0 vs 8.6 +/- 1.7 mumol min-1dl-1, P < 0.05), and a doubling of forearm glucose uptake (0.47 +/- 0.15 to 1.01 +/- 0.28 mumol min-1dl-1, P < 0.05). The latter effect remained significant also when expressed as a ratio to concomitant oxygen balance (0.08 +/- 0.03 vs 0.13 +/- 0.04 mumol mumol-1, P < 0.05), whereas for all other metabolites (lactate, pyruvate, FFA, glycerol, citrate, and beta-hydroxybutyrate) this ratio remained unchanged. During euglycemic hyperinsulinemia, whole-body glucose disposal was stimulated (to 19 +/- 3 mumol min-1kg-1), but forearm blood flow did not increase significantly above baseline (2.9 +/- 0.2 vs 3.1 +/- 0.2 ml min-1dl-1, P = NS). Forearm oxygen balance increased (by 30%, P < 0.05) and forearm glucose uptake rose fourfold (from 0.5 to 2.3 mumol min-1dl-1, P < 0.05). Superimposing an adenosine infusion into one forearm resulted in a 100% increase in blood flow (from 2.9 +/- 0.2 to 6.1 +/- 0.9 ml min-1dl-1, P < 0.001); there was, however, no further stimulation of oxygen or glucose uptake compared with the control forearm. During the clamp, the ratio of glucose to oxygen uptake was similar in the control and in the infused forearms (0.27 +/- 0.11 and 0.23 +/- 0.09, respectively), and was not altered by adenosine (0.31 +/- 0.9 and 0.29 +/- 0.10). We conclude that in insulin-re15-76sistant patients with hypertension, adenosine-induced vasodilation recruits oxidative muscle tissues and exerts a modest, direct metabolic effect to promote muscle glucose uptake in the fasting state. Despite these effects, however, adenosine does not overcome muscle insulin resistance.
Insulin resistance and vasodilation in essential hypertension. Studies with adenosine.
A Natali, R Bonadonna, D Santoro, A Q Galvan, S Baldi, S Frascerra, C Palombo, S Ghione, and E Ferrannini
1994 Oct;
23463013
Phantom pain after arm amputation is widely believed to arise from maladaptive cortical reorganization, triggered by loss of sensory input. We instead propose that chronic phantom pain experience drives plasticity by maintaining local cortical representations and disrupting inter-regional connectivity. Here we show that, while loss of sensory input is generally characterized by structural and functional degeneration in the deprived sensorimotor cortex, the experience of persistent pain is associated with preserved structure and functional organization in the former hand area. Furthermore, consistent with the isolated nature of phantom experience, phantom pain is associated with reduced inter-regional functional connectivity in the primary sensorimotor cortex. We therefore propose that contrary to the maladaptive model, cortical plasticity associated with phantom pain is driven by powerful and long-lasting subjective sensory experience, such as triggered by nociceptive or top-down inputs. Our results prompt a revisiting of the link between phantom pain and brain organization.
Phantom pain is associated with preserved structure and function in the former hand area
Tamar R. Makin,a,1 Jan Scholz,1,2 Nicola Filippini,1,3 David Henderson Slater,4 Irene Tracey,1,5 and Heidi Johansen-Berg1
2013 Mar 5;
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