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anti-Human SCP2 Antikörper:
anti-Mouse (Murine) SCP2 Antikörper:
anti-Rat (Rattus) SCP2 Antikörper:
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Human Polyclonal SCP2 Primary Antibody für IHC (p), IHC - ABIN451521
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 (zeige CTDSP2 Antikörper) domains; (2) identified structure-determined sequence features; (3) compared the lipid binding cavity of SCP2 (zeige CTDSP2 Antikörper) and other lipid binding proteins; (4) surveyed proposed mechanisms of SCP2 (zeige CTDSP2 Antikörper) mediated lipid transfer between membranes; and (5) uncovered a possible new function of the SCP2 (zeige CTDSP2 Antikörper) 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 (zeige CTDSP2 Antikörper) locus present a modulated diurnal accumulation of lipids in the liver and a perturbed activation of several signaling pathways including PPARalpha (zeige PPARA Antikörper), SREBP, LRH-1 (zeige NR5A2 Antikörper), TORC1 (zeige CRTC1 Antikörper) and its upstream regulators.
We conclude that SCP-2 (zeige CTDSP2 Antikörper) 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 (zeige CTDSP2 Antikörper) is autonomous and is essential for binding to pex5 (zeige PEX5 Antikörper).
cellular SCP-2 (zeige CTDSP2 Antikörper) 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 (zeige CTDSP2 Antikörper)) was itself inactive in mediating intermembrane sterol transfer, it nevertheless potentiated the ability of SCP(2 (zeige CTDSP2 Antikörper)) to enhance sterol transfer
SCP2 (zeige CTDSP2 Antikörper) in the cellular defense against oxidative damage and found that a fluorescent fatty acid analog bound to SCP2 (zeige CTDSP2 Antikörper) is protected against H2O2/Cu2+-induced oxidative damage
Overexpression of human SCP-2 (zeige CTDSP2 Antikörper) 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.
Ablating both Fabp1 (zeige FABP1 Antikörper) and Scp2/Scpx (TKO (zeige MRPS12 Antikörper)) induces hepatic phospholipid and cholesterol accumulation in high fat-fed mice
role of Fabp1/Scp (zeige FABP1 Antikörper)-2 (zeige CRISP3 Antikörper) 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 (zeige FABP1 Antikörper).
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 (zeige FABP1 Antikörper) 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 (zeige FABP1 Antikörper) and SCP-2 (zeige CRISP3 Antikörper), 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 (zeige HSD11B1 Antikörper)-cholesterol
liver fatty acid-binding protein, the single most prevalent hepatic cytosolic protein that binds cholesterol, was upregulated twofold in SCP-2 (zeige CRISP3 Antikörper) null hepatocytes
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 (zeige SGMS1 Antikörper) (BODIPY-PC) from donor membranes to acceptor membranes.
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