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anti-Human SCP2 Antikörper:
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Polyclonal SCP2 Primary Antibody für ELISA, WB - ABIN539834
Atshaves, Gallegos, McIntosh, Kier, Schroeder: Sterol carrier protein-2 selectively alters lipid composition and cholesterol dynamics of caveolae/lipid raft vs nonraft domains in L-cell fibroblast plasma membranes. in Biochemistry 2003
We (1) analyzed the structural basis of the fold and the classification of SCP2 domains; (2) identified structure-determined sequence features; (3) compared the lipid binding cavity of SCP2 and other lipid binding proteins; (4) surveyed proposed mechanisms of SCP2 mediated lipid transfer between membranes; and (5) uncovered a possible new function of the SCP2 domain as a protein-protein recognition device.
imported protein sterol carrier protein 2 (SCP2) occupies only a subregion of larger peroxisomes, highlighting the heterogeneous distribution of proteins even within the peroxisome.
Mice harboring a deletion of the Scp2 locus present a modulated diurnal accumulation of lipids in the liver and a perturbed activation of several signaling pathways including PPARalpha, SREBP, LRH-1, TORC1 and its upstream regulators.
We conclude that SCP-2 is a low affinity binding protein for arachidonylethanolamine that can facilitate its cellular uptake but does not contribute significantly to intracellular sequestration of AEA.
The Peroxisomal targeting signal 1 in Scp2 is autonomous and is essential for binding to pex5.
cellular SCP-2 not only binds and translocates cholesterol but also cholesterol hydroperoxides, thus expanding their redox toxicity and signaling ranges under oxidative stress conditions
Statistical analysis indicated that six genes, NFATC2, SCP2, CACNA1C, TCRA, POLE, and FAM3D, were associated with narcolepsy.
data for the first time showed that while the N-terminal membrane binding domain of SCP(2) was itself inactive in mediating intermembrane sterol transfer, it nevertheless potentiated the ability of SCP(2) to enhance sterol transfer
plays a hitherto unrecognized role in intracellular phosphatidylinositol transfer, distribution, and signaling
SCP2 in the cellular defense against oxidative damage and found that a fluorescent fatty acid analog bound to SCP2 is protected against H2O2/Cu2+-induced oxidative damage
Overexpression of human SCP-2 in murine fibroblasts significantly alters the sterol dynamics of caveolae/lipid rafts, but not nonlipid raft domains, to facilitate retention of cholesterol within the cell.
By trafficking cholesterol hydroperoxides and phospholipid hydroperoxides in addition to parent lipids, SCP2 may exacerbate cell injury under oxidative stress conditions
Long chain fatty acyl-coenzyme A (CoA)s are confirmed to be high affinity ligands for SCP2, while long chain fatty acyl-carnitines are demonstrated for the first time not to interact with SCP2.
the importance of the N-terminal presequence in regulating SCP-2 structure, cholesterol localization within the ligand binding site, membrane association, and, potentially, intracellular targeting
Results describe the dynamical effect of sterol carrier protein-2 (SCP-2) interacting between aqueous dispersions of dehydroergosterol monohydrate microcrystal donors and acceptors.
Ablating both Fabp1 and Scp2/Scpx (TKO) induces hepatic phospholipid and cholesterol accumulation in high fat-fed mice
role of Fabp1/Scp-2 in hepatic phytol metabolism
Thus, the loss of Scp-2/Scp-x contributed to a sex-dependent hepatic accumulation of dietary phytol and BCFA.
Individually ablating SCPx or SCP2/SCPx elicited concomitant upregulation of L-FABP.
Lack of a significant decrease in the flux of HDL-[(3)H]CE to biliary FC or bile acids in FABP1(-/-) mice indicates the likely compensation of its function by an as yet unidentified mechanism. Taken together, these studies demonstrate that FABP1 and SCP2 facilitate the preferential movement of HDL-CEs to bile for final elimination
Sterol Carrier Protein-2, a Nonspecific Lipid-Transfer Protein, in Intracellular Cholesterol Trafficking in Testicular Leydig Cells
L-FABP was more important in hepatic retention of bile acids, while SCP-2/SCP-x more broadly affected biliary bile acid and phospholipid levels.
Loss of L-FABP and SCP-2, or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease.
SCP-2/SCP-x may function more in formation and biliary secretion of bile acid, with less impact on hepatic uptake or biliary secretion of HDL-cholesterol
liver fatty acid-binding protein, the single most prevalent hepatic cytosolic protein that binds cholesterol, was upregulated twofold in SCP-2 null hepatocytes
SCP-2 expression plays a significant role in HDL-mediated cholesterol efflux by regulating the size of rapid vs. slow cholesterol efflux pools and/or eliciting concomitant upregulation of L-FABP in cultured primary hepatocytes.
Effect of Scp2 expression on the rate of sterol transfer from lysosomal membranes, and lysosomal membrane lipid distribution.
Data show that expression of sterol carrier protein-2 (SCP-2) increased fatty acid uptake and targeted fatty acid to unique lipid pools, suggesting that SCP-2 may effectively serve as universal fatty acid binding and trafficking protein.
Results suggest a key regulatory role for sterol carrier protein-2 in hepatic lipid metabolism.
SCP-2 contributes to the accumulation of cholesterol in L-FABP null liver
SCP-2 and SCP-x stimulate oxidation and esterification of branched-chain as well as straight-chain fatty acids in intact cells.
Results demonstrate a direct physiological relationship between lack of SCP-x and decreased ability to metabolize branched-chain lipids.
Regulation of the SCPx gene by SF-1 and cAMP is similar to the regulatory mechanisms observed for other steroidogenic genes.
SCP-2/SCP-x has a role in regulating lipid raft domains in primary cultured mouse hepatocytes
Results support an important role for SCP-2 in hepatic cholesterol homeostasis.
Knockdown of scp2 did not interfere with the patterning of the kidney along its proximo-distal axis, but dramatically decreased the size of the kidney, in particular the proximal tubules.
By trafficking cholesterol hydroperoxides and phospholipid hydroperoxides in addition to parent lipids, SCP2 may exacerbate cell injury under oxidative stress conditions. [sterol carrier protein 2, SCP2, nonspecific lipid transfer protein]
Arabidopsis SCP-2 is localised to peroxisomes and showed in vitro transfer activity of BODIPY-phosphatidylcholine (BODIPY-PC) from donor membranes to acceptor membranes.
AtSCP2 is important for the metabolism in A. thaliana seeds and seedlings.
This gene encodes two proteins (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. The transcript initiated from the proximal promoter encodes the longer SCPx protein, and the transcript initiated from the distal promoter encodes the shorter SCP2 protein, with the 2 proteins sharing a common C-terminus. Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein. This gene is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are deficient in peroxisomes and have impaired bile acid synthesis. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms.
non-specific lipid-transfer protein
, propanoyl-CoA C-acyltransferase
, sterol carrier protein X
, nonspecific lipid transfer protein
, Sterol carrier protein 2, liver
, sterol carrier protein 2
, sterol carrier protein-2
, SCP2 (STEROL CARRIER PROTEIN 2); oxidoreductase/ sterol carrier
, allergen Zea m 14
, sterol carrier protein 2, liver