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SCP2 encodes two proteins (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. Additionally we are shipping SCP2 Kits (13) and SCP2 Proteins (13) and many more products for this protein.
Showing 10 out of 122 products:
Human Polyclonal SCP2 Primary Antibody for EIA, IHC (p) - ABIN954693
Dansen, Kops, Denis, Jelluma, Wanders, Bos, Burgering, Wirtz: Regulation of sterol carrier protein gene expression by the forkhead transcription factor FOXO3a. in Journal of lipid research 2004
Show all 5 references for ABIN954693
Human Polyclonal SCP2 Primary Antibody for IHC (p), WB - ABIN656448
Shimada, Miyagawa, Kawashima, Tanaka, Honda, Honda, Tokunaga: An approach based on a genome-wide association study reveals candidate loci for narcolepsy. in Human genetics 2010
Show all 2 references for ABIN656448
Human Polyclonal SCP2 Primary Antibody for EIA, WB - ABIN453819
Baker, Billheimer, Strauss: Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx. in DNA and cell biology 1992
Show all 2 references for ABIN453819
Human Polyclonal SCP2 Primary Antibody for FACS, IHC (p) - ABIN652579
Vila, Levchenko, Korytowski, Girotti: Sterol carrier protein-2-facilitated intermembrane transfer of cholesterol- and phospholipid-derived hydroperoxides. in Biochemistry 2004
Human Polyclonal SCP2 Primary Antibody for WB - ABIN2786761
Stanley, Versluis, Schultz, Heck, Wilmanns: Investigation of the ligand spectrum of human sterol carrier protein 2 using a direct mass spectrometry assay. in Archives of biochemistry and biophysics 2007
Sterol Carrier Protein-2, a Nonspecific Lipid-Transfer Protein, in Intracellular Cholesterol Trafficking in Testicular Leydig Cells
L-FABP (show FABP1 Antibodies) 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 (show FABP1 Antibodies) and SCP-2 (show CRISP3 Antibodies), or both induces hepatic lipid accumulation in female mice and mimics non-alcoholic fatty liver disease.
CTDSP2 (show CTDSP2 Antibodies) induces p21(Cip1/Waf1 (show CDKN1A Antibodies)) through increasing the activity of Ras.
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 (show HSD11B1 Antibodies)-cholesterol
liver fatty acid-binding protein, the single most prevalent hepatic cytosolic protein that binds cholesterol, was upregulated twofold in SCP-2 (show CRISP3 Antibodies) 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 (show CRISP3 Antibodies) 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 (show CRISP3 Antibodies) 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.
We conclude that SCP-2 (show CTDSP2 Antibodies) 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 (show CTDSP2 Antibodies) is autonomous and is essential for binding to pex5 (show PEX5 Antibodies).
cellular SCP-2 (show CTDSP2 Antibodies) 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 (show CTDSP2 Antibodies)) was itself inactive in mediating intermembrane sterol transfer, it nevertheless potentiated the ability of SCP(2 (show CTDSP2 Antibodies)) to enhance sterol transfer
SCP2 (show CTDSP2 Antibodies) in the cellular defense against oxidative damage and found that a fluorescent fatty acid analog bound to SCP2 (show CTDSP2 Antibodies) is protected against H2O2/Cu2+-induced oxidative damage
Overexpression of human SCP-2 (show CTDSP2 Antibodies) 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 (show CTDSP2 Antibodies) may exacerbate cell injury under oxidative stress conditions
Long chain fatty acyl-coenzyme A (show SOAT2 Antibodies) (CoA)s are confirmed to be high affinity ligands for SCP2 (show CTDSP2 Antibodies), while long chain fatty acyl-carnitines are demonstrated for the first time not to interact with SCP2 (show CTDSP2 Antibodies).
the importance of the N-terminal presequence in regulating SCP-2 (show CTDSP2 Antibodies) structure, cholesterol localization within the ligand binding site, membrane association, and, potentially, intracellular targeting
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]
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.
carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
, nuclear LIM interactor-interacting factor 2 (NLI-interacting factor 2) (Protein OS-4)
, small C-terminal domain phosphatase 2
, allergen Zea m 14
, non-specific lipid-transfer protein
, propanoyl-CoA C-acyltransferase
, sterol carrier protein X
, Sterol carrier protein 2, liver
, sterol carrier protein-2
, sterol carrier protein 2, liver
, nonspecific lipid transfer protein