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貨期:
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用途:
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.; Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol. Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.
基因功能參考文獻:
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. PMID: 28284963
imported protein sterol carrier protein 2 (SCP2) occupies only a subregion of larger peroxisomes, highlighting the heterogeneous distribution of proteins even within the peroxisome. PMID: 27311714
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. PMID: 27097688
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. PMID: 24510313
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 PMID: 20656919
Statistical analysis indicated that six genes, NFATC2, SCP2, CACNA1C, TCRA, POLE, and FAM3D, were associated with narcolepsy. PMID: 20677014
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 PMID: 12356316
plays a hitherto unrecognized role in intracellular phosphatidylinositol transfer, distribution, and signaling PMID: 12641450
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 PMID: 14563822
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. PMID: 14661971
By trafficking cholesterol hydroperoxides and phospholipid hydroperoxides in addition to parent lipids, SCP2 may exacerbate cell injury under oxidative stress conditions PMID: 15449949
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. PMID: 17418802
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 PMID: 18465878
Results describe the dynamical effect of sterol carrier protein-2 (SCP-2) interacting between aqueous dispersions of dehydroergosterol monohydrate microcrystal donors and acceptors. PMID: 19020914
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相關疾病:
Leukoencephalopathy with dystonia and motor neuropathy (LKDMN)