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Human Monoclonal SLC27A2 Primary Antibody für IHC, ELISA - ABIN1724864
Mishima, Miner, Morizane, Stahl, Sadovsky: The expression and function of fatty acid transport protein-2 and -4 in the murine placenta. in PLoS ONE 2011
Show all 2 Pubmed References
We conclude that FATP2 is a major apical proximal tubule NEFA transporter that regulates lipoapoptosis and may be an amenable target for the prevention of CKD progression.
SLC27A2 is required for the transcriptional induction of miR-411 in ovarian cancer. Reduced miR-411 expression contributes to ovarian cancer chemo-resistance.
Contractile strength in FATP2-knockdown gallbladders was significantly greater than in control gallbladders following lithogenic diet administration. FATP2-knockdown significantly reduced gallbladder triacylglycerol.
In mice Grassofermata decreased absorption of (13)C-oleate demonstrating its potential as a therapeutic agent.
even though hypoxia regulates the expression of FATP2 and FATP4 in human trophoblasts, mouse Fatp2 and Fatp4 are not essential for intrauterine fetal growth
FATP2 is a multifunctional protein that shows subcellular localization-dependent activity and is a major contributor ro peroxisomal (V)LACS activity.
mouse VLCS gene (Vlcs) encodes an enzyme (Vlcs) with VLCS activity that localizes to peroxisomes and is expressed in X-ALD target tissues
PPARalpha up-regulates the expression of Slc27a2 in small intestine.
In overweight/obese pregnancies, the increased FATP2 placental expression could contribute to increased fatty acid delivery to the fetus.
Protective effects of breastfeeding are reflected in higher expression levels of SLC27A2, FASN, PPARalpha and INSR in blood cells.
these data support the conclusion that FATP2 has a dual function in the pathways linking the transport and activation of exogenous fatty acids.
even though hypoxia regulates the expression of FATP2 and FATP4 in human trophoblasts, mouse Fatp2 and Fatp4 are not essential for intrauterine fetal growth.
FATP2a functions in fatty acid transport and activation and provides specificity toward n-3 fatty acids in which the corresponding n-3 acyl-CoAs are preferentially trafficked into acyl-CoA pools destined for phosphatidylinositol incorporation
The protein encoded by this gene is an isozyme of long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. This isozyme activates long-chain, branched-chain and very-long-chain fatty acids containing 22 or more carbons to their CoA derivatives. It is expressed primarily in liver and kidney, and is present in both endoplasmic reticulum and peroxisomes, but not in mitochondria. Its decreased peroxisomal enzyme activity is in part responsible for the biochemical pathology in X-linked adrenoleukodystrophy. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
solute carrier family 27 (fatty acid transporter), member 2
, solute carrier family 27 (fatty acid transporter) member 2
, solute carrier family 27 member 2
, THCA-CoA ligase
, fatty acid transport protein 2
, fatty-acid-coenzyme A ligase, very long-chain 1
, long-chain-fatty-acid--CoA ligase
, very long-chain acyl-CoA synthetase
, very long-chain acyl-Coenzyme A dehydrogenase synthase
, very long-chain-fatty-acid-CoA ligase
, solute carrier family 27 (fatty acid transporter), member 32
, very long-chain fatty-acid-coenzyme A ligase 1
, very-long-chain acyl-CoA synthetase