There are 2+ publications for this product available. The Mouse Monoclonal anti-SLC27A2 antibody is suitable to detect SLC27A2 in samples from Human. It has been validated for ELISA and IHC.
SLC27A2
Reactivity: Human
ELISA
Host: Rabbit
Polyclonal
unconjugated
Application Notes
ELISA: 1/10000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified antibody in PBS with 0.05 % sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Storage Comment
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Mishima, Miner, Morizane, Stahl, Sadovsky: "The expression and function of fatty acid transport protein-2 and -4 in the murine placenta." in: PLoS ONE, Vol. 6, Issue 10, pp. e25865, (2011) (PubMed).
Campa, Hüsing, Chang-Claude, Dostal, Boeing, Kröger, Tjønneland, Roswall, Overvad, Dahm, Rodríguez, Sala, Pérez, Larrañaga, Chirlaque, Ardanaz, Khaw, Wareham, Allen, Travis, Trichopoulou, Naska et al.: "Genetic variability of the fatty acid synthase pathway is not associated with prostate cancer risk in the European Prospective Investigation on Cancer (EPIC). ..." in: European journal of cancer (Oxford, England : 1990), Vol. 47, Issue 3, pp. 420-7, (2011) (PubMed).
Target
SLC27A2
(Solute Carrier Family 27 (Fatty Acid Transporter), Member 2 (SLC27A2))
Alternative Name
SLC27A2
Background
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.