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The antibody against SLC27A2 was raised in rabbit using the Recombinant Human Very long-chain acyl-CoA synthetase protein (283-620AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.
The antibody against SLC27A2 was raised in rabbit using the Recombinant Human Very long-chain acyl-CoA synthetase protein (283-620AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.
$299.00
| Cat.No | ADC-50071A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | SLC27A2 |
| Target Synonyms | ACSVL1 antibody; FACVL1 antibody; FATP 2 antibody; FATP-2 antibody; FATP2 antibody; Fatty acid coenzyme A ligase | Form | Liquid |
| Species Reactivity | Human | Isotype | IgG |
| Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 | Purification Method | >95%, Protein G purified |
| Conjugate | Non-conjugated | Application | ELISA |
| Storage | Upon receipt |
| Immunogen Description | Recombinant Human Very long-chain acyl-CoA synthetase protein (283-620AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | O14975 |
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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