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Rabbit anti-Human SLC27A2 Polyclonal Antibody

The antibody against SLC27A2 was raised in rabbit using the Recombinant Human Very long-chain acyl-CoA synthetase protein (30-200AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA.

ADC-40340A

The antibody against SLC27A2 was raised in rabbit using the Recombinant Human Very long-chain acyl-CoA synthetase protein (30-200AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA.

$299.00

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Specifications


Cat.No ADC-40340A ClonalityPolyclonal
Host SpeciesRabbitTarget NameSLC27A2
Target SynonymsACSVL1 antibody; FACVL1 antibody; FATP 2 antibody; FATP-2 antibody; FATP2 antibody; Fatty acid coenzyme A ligaseFormLiquid
Species ReactivityHumanIsotypeIgG
Storage Buffer50% Glycerol, PBS with 0.02% sodium azide, pH7.3.Purification MethodAntigen affinity purified
ConjugateNon-conjugatedApplicationELISA
StorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Human Very long-chain acyl-CoA synthetase protein (30-200AA)Target SpeciesHuman
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDO14975
Background Information
  • Uniprot Id

    O14975

  • Target Species

    Human

  • Target Name

    SLC27A2

  • Target Full Name

    Long-chain fatty acid transport protein 2

  • Target Function

    Acyl CoA synthetase that activates long-chain and very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid. Does not activate C24 bile acids, cholate and chenodeoxycholate. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Exhibits long-chain fatty acids (LCFA) transport activity and plays an important role in hepatic fatty acid uptake.; Exhibits both long-chain fatty acids (LCFA) transport activity and acyl CoA synthetase towards very long-chain fatty acids. Shows a preference for generating CoA derivatives of n-3 fatty acids, which are preferentially trafficked into phosphatidylinositol.; Exhibits long-chain fatty acids (LCFA) transport activity but lacks acyl CoA synthetase towards very long-chain fatty acids.

  • Target Subcellular Location

    Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Peripheral membrane protein. Cell membrane; Multi-pass membrane protein. Microsome.

  • Target Protein Families

    ATP-dependent AMP-binding enzyme family

  • Target Tissue Specificity

    Expressed in liver, kidney, placenta and pancreas.

  • Target Research Area

    Metabolism

  • Target Synonyms

    ACSVL1; FACVL1; FATP 2; FATP-2; FATP2; Fatty acid coenzyme A ligase, very long chain 1; Fatty acid transport protein 2; Fatty-acid-coenzyme A ligase; hFACVL1; HsT17226; Long chain fatty acid CoA ligase; Long-chain-fatty-acid--CoA ligase; S27A2_HUMAN; Slc27a2; Solute carrier family 27 (fatty acid transporter), member 2; Solute carrier family 27 member 2; THCA CoA ligase; THCA-CoA ligase; Very long chain acyl CoA synthetase; Very long chain fatty acid CoA ligase; Very long chain fatty acid coenzyme A ligase 1; very long-chain 1; Very long-chain acyl-CoA synthetase; Very long-chain-fatty-acid-CoA ligase; VLACS; VLCS

  • Target 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.

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